RS13_ECOLI
ID RS13_ECOLI Reviewed; 118 AA.
AC P0A7S9; P02369; Q2M6W3;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=30S ribosomal protein S13;
DE AltName: Full=Small ribosomal subunit protein uS13 {ECO:0000303|PubMed:24524803};
GN Name=rpsM; OrderedLocusNames=b3298, JW3260;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2989779; DOI=10.1093/nar/13.11.3891;
RA Bedwell D.M., Davis G.R., Gosink M., Post L.E., Nomura M., Kestler H.,
RA Zengel J.M., Lindahl L.;
RT "Nucleotide sequence of the alpha ribosomal protein operon of Escherichia
RT coli.";
RL Nucleic Acids Res. 13:3891-3903(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP PROTEIN SEQUENCE OF 2-118, AND SUBUNIT.
RC STRAIN=K;
RX PubMed=330375; DOI=10.1515/bchm2.1977.358.2.843;
RA Lindemann H., Wittmann-Liebold B.;
RT "Primary structure of protein S13 from the small subunit of Escherichia
RT coli ribosomes.";
RL Hoppe-Seyler's Z. Physiol. Chem. 358:843-863(1977).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
RX PubMed=6154696; DOI=10.1016/s0021-9258(19)85544-8;
RA Post L.E., Arfsten A.E., Davis G.R., Nomura M.;
RT "DNA sequence of the promoter region for the alpha ribosomal protein operon
RT in Escherichia coli.";
RL J. Biol. Chem. 255:4653-4659(1980).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
RX PubMed=6793240; DOI=10.1016/0092-8674(81)90185-9;
RA Miura A., Krueger J.H., Itoh S., de Boer H.A., Nomura M.;
RT "Growth-rate-dependent regulation of ribosome synthesis in E. coli:
RT expression of the lacZ and galK genes fused to ribosomal promoters.";
RL Cell 25:773-782(1981).
RN [7]
RP PROTEIN SEQUENCE OF 83-85, CROSS-LINKING TO S19, AND SUBUNIT.
RC STRAIN=K12 / A19;
RX PubMed=3279034; DOI=10.1016/s0021-9258(18)68924-0;
RA Pohl T., Wittmann-Liebold B.;
RT "Identification of a cross-link in the Escherichia coli ribosomal protein
RT pair S13-S19 at the amino acid level.";
RL J. Biol. Chem. 263:4293-4301(1988).
RN [8]
RP NOMENCLATURE.
RX PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
RA Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT "A new system for naming ribosomal proteins.";
RL Curr. Opin. Struct. Biol. 24:165-169(2014).
RN [9]
RP CHARACTERIZATION OF VARIANT RPSM413.
RC STRAIN=K12;
RX PubMed=8193163; DOI=10.1016/0167-4781(94)90097-3;
RA Faxen M., Walles-Granberg A., Isaksson L.A.;
RT "Antisuppression by a mutation in rpsM(S13) giving a shortened ribosomal
RT protein S13.";
RL Biochim. Biophys. Acta 1218:27-34(1994).
RN [10]
RP CROSS-LINKING TO THE TRNA CENTRAL FOLD, AND SUBUNIT.
RC STRAIN=MRE-600;
RX PubMed=8524654; DOI=10.1093/nar/23.22.4635;
RA Osswald M., Doering T., Brimacombe R.;
RT "The ribosomal neighbourhood of the central fold of tRNA: cross-links from
RT position 47 of tRNA located at the A, P or E site.";
RL Nucleic Acids Res. 23:4635-4641(1995).
RN [11]
RP ABILITY OF VARIANTS PW118; PW097 AND PW095 TO PARTIALLY SUPPRESS A RIMM
RP DELETION.
RC STRAIN=MW100;
RX PubMed=9226267; DOI=10.1128/jb.179.14.4567-4574.1997;
RA Bylund G.O., Persson B.C., Lundberg L.A., Wikstroem P.M.;
RT "A novel ribosome-associated protein is important for efficient translation
RT in Escherichia coli.";
RL J. Bacteriol. 179:4567-4574(1997).
RN [12]
RP ROLE IN P SITE TRNA-BINDING, AND MUTAGENESIS OF 83-LEU--LYS-118 AND
RP 114-LYS--LYS-118.
RC STRAIN=CSH142;
RX PubMed=15308780; DOI=10.1073/pnas.0405227101;
RA Hoang L., Fredrick K., Noller H.F.;
RT "Creating ribosomes with an all-RNA 30S subunit P site.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:12439-12443(2004).
RN [13]
RP MASS SPECTROMETRY, AND SUBUNIT.
RC STRAIN=K12 / ATCC 25404 / DSM 5698 / NCIMB 11290;
RX PubMed=10094780; DOI=10.1006/abio.1998.3077;
RA Arnold R.J., Reilly J.P.;
RT "Observation of Escherichia coli ribosomal proteins and their
RT posttranslational modifications by mass spectrometry.";
RL Anal. Biochem. 269:105-112(1999).
RN [14]
RP 3D-STRUCTURE MODELING, AND SUBUNIT.
RX PubMed=12244297; DOI=10.1038/nsb841;
RA Tung C.-S., Joseph S., Sanbonmatsu K.Y.;
RT "All-atom homology model of the Escherichia coli 30S ribosomal subunit.";
RL Nat. Struct. Biol. 9:750-755(2002).
RN [15]
RP STRUCTURE BY ELECTRON MICROSCOPY (11.50 ANGSTROMS), SUBUNIT, AND
RP INTERSUBUNIT BRIDGE FORMATION.
RC STRAIN=MRE-600;
RX PubMed=12809609; DOI=10.1016/s0092-8674(03)00427-6;
RA Gao H., Sengupta J., Valle M., Korostelev A., Eswar N., Stagg S.M.,
RA Van Roey P., Agrawal R.K., Harvey S.C., Sali A., Chapman M.S., Frank J.;
RT "Study of the structural dynamics of the E. coli 70S ribosome using real-
RT space refinement.";
RL Cell 113:789-801(2003).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (3.46 ANGSTROMS) OF 2 DIFFERENT RIBOSOME STRUCTURES
RP INCLUDING THE INTERSUBUNIT BRIDGE B1B, AND SUBUNIT.
RC STRAIN=MRE-600;
RX PubMed=16272117; DOI=10.1126/science.1117230;
RA Schuwirth B.S., Borovinskaya M.A., Hau C.W., Zhang W., Vila-Sanjurjo A.,
RA Holton J.M., Cate J.H.D.;
RT "Structures of the bacterial ribosome at 3.5 A resolution.";
RL Science 310:827-834(2005).
RN [17]
RP 3D-STRUCTURE MODELING OF RIBOSOMAL COMPLEXES INCLUDING BRIDGE CHANGES UPON
RP TRANSLOCATION, AND SUBUNIT.
RX PubMed=12859903; DOI=10.1016/s0092-8674(03)00476-8;
RA Valle M., Zavialov A., Sengupta J., Rawat U., Ehrenberg M., Frank J.;
RT "Locking and unlocking of ribosomal motions.";
RL Cell 114:123-134(2003).
RN [18]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.0 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX
RP WITH ARFA AND RF2, AND SUBUNIT.
RX PubMed=27906160; DOI=10.1038/nature20822;
RA Ma C., Kurita D., Li N., Chen Y., Himeno H., Gao N.;
RT "Mechanistic insights into the alternative translation termination by ArfA
RT and RF2.";
RL Nature 541:550-553(2017).
RN [19]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.1 ANGSTROMS) OF 70S RIBOSOME IN COMPLEX
RP WITH ARFA AND RF2, AND SUBUNIT.
RX PubMed=27906161; DOI=10.1038/nature20821;
RA Huter P., Mueller C., Beckert B., Arenz S., Berninghausen O., Beckmann R.,
RA Wilson D.N.;
RT "Structural basis for ArfA-RF2-mediated translation termination on mRNAs
RT lacking stop codons.";
RL Nature 541:546-549(2017).
RN [20]
RP STRUCTURE BY ELECTRON MICROSCOPY (2.97 ANGSTROMS) OF 70S RIBOSOME IN
RP COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
RX PubMed=27934701; DOI=10.1126/science.aai9127;
RA James N.R., Brown A., Gordiyenko Y., Ramakrishnan V.;
RT "Translational termination without a stop codon.";
RL Science 354:1437-1440(2016).
RN [21]
RP STRUCTURE BY ELECTRON MICROSCOPY (3.52 ANGSTROMS) OF 70S RIBOSOME IN
RP COMPLEX WITH ARFA AND RF2, AND SUBUNIT.
RX PubMed=28077875; DOI=10.1038/nature21053;
RA Zeng F., Chen Y., Remis J., Shekhar M., Phillips J.C., Tajkhorshid E.,
RA Jin H.;
RT "Structural basis of co-translational quality control by ArfA and RF2 bound
RT to ribosome.";
RL Nature 541:554-557(2017).
CC -!- FUNCTION: Located at the top of the head of the 30S subunit, it
CC contacts several helices of the 16S rRNA.
CC {ECO:0000269|PubMed:15308780}.
CC -!- FUNCTION: In the E.coli 70S ribosome in the initiation state
CC (PubMed:12809609) was modeled to contact the 23S rRNA (bridge B1a) and
CC protein L5 of the 50S subunit (bridge B1b), connecting the 2 subunits;
CC bridge B1a is broken in the model with bound EF-G, while the protein-
CC protein contacts between S13 and L5 in B1b change (PubMed:12809609).
CC The 23S rRNA contact site in bridge B1a is modeled to differ in
CC different ribosomal states (PubMed:16272117), contacting alternately
CC S13 or S19. In the two 3.5 angstroms resolved ribosome structures
CC (PubMed:12859903) the contacts between L5, S13 and S19 bridge B1b are
CC different, confirming the dynamic nature of this interaction. Bridge
CC B1a is not visible in the crystallized ribosomes due to 23S rRNA
CC disorder. {ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:12859903,
CC ECO:0000269|PubMed:15308780, ECO:0000269|PubMed:16272117}.
CC -!- FUNCTION: Contacts the tRNAs in the A and P sites.
CC {ECO:0000269|PubMed:15308780}.
CC -!- FUNCTION: The C-terminal tail plays a role in the affinity of the 30S P
CC site for different tRNAs. {ECO:0000269|PubMed:15308780}.
CC -!- SUBUNIT: Part of the 30S ribosomal subunit (PubMed:330375,
CC PubMed:3279034, PubMed:10094780, PubMed:12809609, PubMed:16272117,
CC PubMed:12859903, PubMed:27934701, PubMed:12244297, PubMed:27906160,
CC PubMed:27906161). Forms a loose heterodimer with protein S19
CC (PubMed:3279034). Cross-links to the P site tRNA and weakly to the A
CC site tRNA (PubMed:8524654). Forms two bridges to the 50S subunit in the
CC 70S ribosome, contacting the 16S rRNA and proteins S19 and L5
CC (PubMed:12809609, PubMed:16272117, PubMed:12859903).
CC {ECO:0000269|PubMed:10094780, ECO:0000269|PubMed:12244297,
CC ECO:0000269|PubMed:12809609, ECO:0000269|PubMed:12859903,
CC ECO:0000269|PubMed:16272117, ECO:0000269|PubMed:27906160,
CC ECO:0000269|PubMed:27906161, ECO:0000269|PubMed:27934701,
CC ECO:0000269|PubMed:3279034, ECO:0000269|PubMed:330375,
CC ECO:0000269|PubMed:8524654}.
CC -!- MASS SPECTROMETRY: Mass=12968.1; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10094780};
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uS13 family.
CC {ECO:0000305}.
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DR EMBL; X02543; CAA26392.1; -; Genomic_DNA.
DR EMBL; U18997; AAA58093.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76323.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77993.1; -; Genomic_DNA.
DR EMBL; M12432; AAA83903.1; -; Genomic_DNA.
DR EMBL; M10213; AAA72457.1; -; Genomic_DNA.
DR PIR; A23807; R3EC13.
DR RefSeq; NP_417757.1; NC_000913.3.
DR RefSeq; WP_000090775.1; NZ_STEB01000038.1.
DR PDB; 2YKR; EM; 9.80 A; M=2-115.
DR PDB; 3J9Y; EM; 3.90 A; m=1-118.
DR PDB; 3J9Z; EM; 3.60 A; SM=2-118.
DR PDB; 3JA1; EM; 3.60 A; SM=2-118.
DR PDB; 3JBU; EM; 3.64 A; M=1-118.
DR PDB; 3JBV; EM; 3.32 A; M=1-118.
DR PDB; 3JCD; EM; 3.70 A; m=1-118.
DR PDB; 3JCE; EM; 3.20 A; m=1-118.
DR PDB; 3JCJ; EM; 3.70 A; s=1-118.
DR PDB; 3JCN; EM; 4.60 A; n=1-118.
DR PDB; 4A2I; EM; 16.50 A; M=2-115.
DR PDB; 4ADV; EM; 13.50 A; M=2-118.
DR PDB; 4U1U; X-ray; 2.95 A; AM/CM=2-115.
DR PDB; 4U1V; X-ray; 3.00 A; AM/CM=2-115.
DR PDB; 4U20; X-ray; 2.90 A; AM/CM=2-115.
DR PDB; 4U24; X-ray; 2.90 A; AM/CM=2-115.
DR PDB; 4U25; X-ray; 2.90 A; AM/CM=2-115.
DR PDB; 4U26; X-ray; 2.80 A; AM/CM=2-115.
DR PDB; 4U27; X-ray; 2.80 A; AM/CM=2-115.
DR PDB; 4V47; EM; 12.30 A; BM=2-118.
DR PDB; 4V48; EM; 11.50 A; BM=2-118.
DR PDB; 4V4H; X-ray; 3.46 A; AM/CM=1-118.
DR PDB; 4V4Q; X-ray; 3.46 A; AM/CM=2-118.
DR PDB; 4V4V; EM; 15.00 A; AM=2-116.
DR PDB; 4V4W; EM; 15.00 A; AM=2-116.
DR PDB; 4V50; X-ray; 3.22 A; AM/CM=2-118.
DR PDB; 4V52; X-ray; 3.21 A; AM/CM=2-118.
DR PDB; 4V53; X-ray; 3.54 A; AM/CM=2-118.
DR PDB; 4V54; X-ray; 3.30 A; AM/CM=2-118.
DR PDB; 4V55; X-ray; 4.00 A; AM/CM=2-118.
DR PDB; 4V56; X-ray; 3.93 A; AM/CM=2-118.
DR PDB; 4V57; X-ray; 3.50 A; AM/CM=2-118.
DR PDB; 4V5B; X-ray; 3.74 A; BM/DM=2-118.
DR PDB; 4V5H; EM; 5.80 A; AM=2-114.
DR PDB; 4V5Y; X-ray; 4.45 A; AM/CM=2-118.
DR PDB; 4V64; X-ray; 3.50 A; AM/CM=2-118.
DR PDB; 4V65; EM; 9.00 A; AF=1-118.
DR PDB; 4V66; EM; 9.00 A; AF=1-118.
DR PDB; 4V69; EM; 6.70 A; AM=2-114.
DR PDB; 4V6C; X-ray; 3.19 A; AM/CM=1-118.
DR PDB; 4V6D; X-ray; 3.81 A; AM/CM=1-118.
DR PDB; 4V6E; X-ray; 3.71 A; AM/CM=1-118.
DR PDB; 4V6K; EM; 8.25 A; BQ=1-118.
DR PDB; 4V6L; EM; 13.20 A; AQ=1-118.
DR PDB; 4V6N; EM; 12.10 A; BP=2-118.
DR PDB; 4V6O; EM; 14.70 A; AP=2-118.
DR PDB; 4V6P; EM; 13.50 A; AP=2-118.
DR PDB; 4V6Q; EM; 11.50 A; AP=2-118.
DR PDB; 4V6R; EM; 11.50 A; AP=2-118.
DR PDB; 4V6S; EM; 13.10 A; BO=2-118.
DR PDB; 4V6T; EM; 8.30 A; AM=2-115.
DR PDB; 4V6V; EM; 9.80 A; AM=2-118.
DR PDB; 4V6Y; EM; 12.00 A; AM=1-114.
DR PDB; 4V6Z; EM; 12.00 A; AM=1-114.
DR PDB; 4V70; EM; 17.00 A; AM=1-114.
DR PDB; 4V71; EM; 20.00 A; AM=1-114.
DR PDB; 4V72; EM; 13.00 A; AM=1-114.
DR PDB; 4V73; EM; 15.00 A; AM=1-114.
DR PDB; 4V74; EM; 17.00 A; AM=1-114.
DR PDB; 4V75; EM; 12.00 A; AM=1-114.
DR PDB; 4V76; EM; 17.00 A; AM=1-114.
DR PDB; 4V77; EM; 17.00 A; AM=1-114.
DR PDB; 4V78; EM; 20.00 A; AM=1-114.
DR PDB; 4V79; EM; 15.00 A; AM=1-114.
DR PDB; 4V7A; EM; 9.00 A; AM=1-114.
DR PDB; 4V7B; EM; 6.80 A; AM=1-118.
DR PDB; 4V7C; EM; 7.60 A; AM=2-118.
DR PDB; 4V7D; EM; 7.60 A; BM=2-118.
DR PDB; 4V7I; EM; 9.60 A; BM=1-118.
DR PDB; 4V7S; X-ray; 3.25 A; AM=2-115, CM=2-114.
DR PDB; 4V7T; X-ray; 3.19 A; AM=2-115, CM=2-114.
DR PDB; 4V7U; X-ray; 3.10 A; AM/CM=2-115.
DR PDB; 4V7V; X-ray; 3.29 A; AM=2-115, CM=2-114.
DR PDB; 4V85; X-ray; 3.20 A; AM=1-118.
DR PDB; 4V89; X-ray; 3.70 A; AM=1-118.
DR PDB; 4V9C; X-ray; 3.30 A; AM/CM=1-118.
DR PDB; 4V9D; X-ray; 3.00 A; AM/BM=2-115.
DR PDB; 4V9O; X-ray; 2.90 A; BM/DM/FM/HM=1-118.
DR PDB; 4V9P; X-ray; 2.90 A; BM/DM/FM/HM=1-118.
DR PDB; 4WF1; X-ray; 3.09 A; AM/CM=2-115.
DR PDB; 4WOI; X-ray; 3.00 A; AM/DM=1-118.
DR PDB; 4WWW; X-ray; 3.10 A; QM/XM=2-115.
DR PDB; 4YBB; X-ray; 2.10 A; AM/BM=2-115.
DR PDB; 5AFI; EM; 2.90 A; m=1-118.
DR PDB; 5H5U; EM; 3.00 A; t=2-118.
DR PDB; 5IQR; EM; 3.00 A; r=1-118.
DR PDB; 5IT8; X-ray; 3.12 A; AM/BM=2-115.
DR PDB; 5J5B; X-ray; 2.80 A; AM/BM=2-115.
DR PDB; 5J7L; X-ray; 3.00 A; AM/BM=2-115.
DR PDB; 5J88; X-ray; 3.32 A; AM/BM=2-115.
DR PDB; 5J8A; X-ray; 3.10 A; AM/BM=2-115.
DR PDB; 5J91; X-ray; 2.96 A; AM/BM=2-115.
DR PDB; 5JC9; X-ray; 3.03 A; AM/BM=2-115.
DR PDB; 5JTE; EM; 3.60 A; AM=1-118.
DR PDB; 5JU8; EM; 3.60 A; AM=1-118.
DR PDB; 5KCR; EM; 3.60 A; 1m=1-118.
DR PDB; 5KCS; EM; 3.90 A; 1m=1-118.
DR PDB; 5KPS; EM; 3.90 A; 18=1-118.
DR PDB; 5KPV; EM; 4.10 A; 17=1-118.
DR PDB; 5KPW; EM; 3.90 A; 17=1-118.
DR PDB; 5KPX; EM; 3.90 A; 17=1-118.
DR PDB; 5L3P; EM; 3.70 A; m=1-118.
DR PDB; 5LZA; EM; 3.60 A; m=2-115.
DR PDB; 5LZB; EM; 5.30 A; m=2-115.
DR PDB; 5LZC; EM; 4.80 A; m=2-115.
DR PDB; 5LZD; EM; 3.40 A; m=2-115.
DR PDB; 5LZE; EM; 3.50 A; m=2-115.
DR PDB; 5LZF; EM; 4.60 A; m=2-115.
DR PDB; 5MDV; EM; 2.97 A; r=1-118.
DR PDB; 5MDW; EM; 3.06 A; r=1-118.
DR PDB; 5MDY; EM; 3.35 A; r=1-118.
DR PDB; 5MDZ; EM; 3.10 A; r=1-118.
DR PDB; 5ME0; EM; 13.50 A; M=1-118.
DR PDB; 5ME1; EM; 13.50 A; M=1-118.
DR PDB; 5MGP; EM; 3.10 A; m=2-115.
DR PDB; 5MY1; EM; 7.60 A; M=2-118.
DR PDB; 5NO2; EM; 5.16 A; M=2-115.
DR PDB; 5NO3; EM; 5.16 A; M=2-115.
DR PDB; 5NO4; EM; 5.16 A; M=2-115.
DR PDB; 5NP6; EM; 3.60 A; P=2-115.
DR PDB; 5NWY; EM; 2.93 A; C=1-118.
DR PDB; 5O2R; EM; 3.40 A; m=2-115.
DR PDB; 5U4I; EM; 3.50 A; m=1-118.
DR PDB; 5U9F; EM; 3.20 A; M=1-118.
DR PDB; 5U9G; EM; 3.20 A; M=1-118.
DR PDB; 5UYK; EM; 3.90 A; M=2-115.
DR PDB; 5UYL; EM; 3.60 A; M=2-115.
DR PDB; 5UYM; EM; 3.20 A; M=2-115.
DR PDB; 5UYN; EM; 4.00 A; M=2-115.
DR PDB; 5UYP; EM; 3.90 A; M=2-115.
DR PDB; 5UYQ; EM; 3.80 A; M=2-115.
DR PDB; 5UZ4; EM; 5.80 A; M=1-118.
DR PDB; 5WDT; EM; 3.00 A; m=2-116.
DR PDB; 5WE4; EM; 3.10 A; m=2-116.
DR PDB; 5WE6; EM; 3.40 A; m=2-115.
DR PDB; 5WFK; EM; 3.40 A; m=2-116.
DR PDB; 6BU8; EM; 3.50 A; M=2-115.
DR PDB; 6BY1; X-ray; 3.94 A; AM/BM=2-115.
DR PDB; 6C4I; EM; 3.24 A; m=1-118.
DR PDB; 6DNC; EM; 3.70 A; ZA=1-118.
DR PDB; 6ENF; EM; 3.20 A; m=2-115.
DR PDB; 6ENJ; EM; 3.70 A; m=2-115.
DR PDB; 6ENU; EM; 3.10 A; m=2-115.
DR PDB; 6GWT; EM; 3.80 A; m=2-115.
DR PDB; 6GXM; EM; 3.80 A; m=2-115.
DR PDB; 6GXN; EM; 3.90 A; m=2-115.
DR PDB; 6GXO; EM; 3.90 A; m=2-115.
DR PDB; 6GXP; EM; 4.40 A; m=2-115.
DR PDB; 6H4N; EM; 3.00 A; m=2-115.
DR PDB; 6H58; EM; 7.90 A; m/mm=2-115.
DR PDB; 6HRM; EM; 2.96 A; r=2-117.
DR PDB; 6I7V; X-ray; 2.90 A; AM/BM=2-115.
DR PDB; 6O9J; EM; 3.90 A; m=2-115.
DR PDB; 6O9K; EM; 4.00 A; m=2-115.
DR PDB; 6OFX; EM; 3.30 A; R=2-115.
DR PDB; 6OG7; EM; 3.30 A; R=2-115.
DR PDB; 6ORE; EM; 2.90 A; r=2-117.
DR PDB; 6ORL; EM; 3.50 A; r=2-117.
DR PDB; 6OST; EM; 4.20 A; r=2-117.
DR PDB; 6OT3; EM; 3.90 A; r=2-117.
DR PDB; 6OUO; EM; 3.70 A; r=2-117.
DR PDB; 6Q98; EM; 4.30 A; r=1-118.
DR PDB; 6Q9A; EM; 3.70 A; r=2-117.
DR PDB; 6SZS; EM; 3.06 A; m=1-118.
DR PDB; 6TBV; EM; 2.70 A; S131=1-118.
DR PDB; 6TC3; EM; 2.70 A; S131=1-118.
DR PDB; 6VWL; EM; 3.10 A; l=1-118.
DR PDB; 6VWM; EM; 3.40 A; l=1-118.
DR PDB; 6VWN; EM; 3.40 A; l=1-118.
DR PDB; 6W6K; EM; 3.60 A; M=1-118.
DR PDB; 6W77; EM; 3.60 A; M=1-118.
DR PDB; 6W7M; EM; 3.80 A; M=1-118.
DR PDB; 6W7N; EM; 3.40 A; M=1-118.
DR PDB; 6WD6; EM; 3.70 A; R=2-115.
DR PDB; 6WDB; EM; 4.00 A; R=2-115.
DR PDB; 6WDC; EM; 4.20 A; R=2-115.
DR PDB; 6WDD; EM; 3.20 A; R=2-115.
DR PDB; 6WDE; EM; 3.00 A; R=2-115.
DR PDB; 6WDF; EM; 3.30 A; R=2-115.
DR PDB; 6WDG; EM; 3.30 A; R=2-115.
DR PDB; 6WDH; EM; 4.30 A; R=2-115.
DR PDB; 6WDI; EM; 4.00 A; R=2-115.
DR PDB; 6WDJ; EM; 3.70 A; R=2-115.
DR PDB; 6WDK; EM; 3.60 A; R=2-115.
DR PDB; 6WDL; EM; 3.70 A; R=2-115.
DR PDB; 6WDM; EM; 3.60 A; R=2-115.
DR PDB; 6WNV; EM; 3.50 A; R=2-115.
DR PDB; 6WNW; EM; 3.20 A; R=2-115.
DR PDB; 6XE0; EM; 6.80 A; L=2-115.
DR PDB; 6XZA; EM; 2.66 A; M1=2-115.
DR PDB; 6XZB; EM; 2.54 A; M1=2-115.
DR PDB; 6Y69; EM; 2.86 A; m=2-115.
DR PDB; 6ZTL; EM; 3.50 A; AM=1-118.
DR PDB; 7ABZ; EM; 3.21 A; r=2-115.
DR PDB; 7AC7; EM; 3.08 A; r=2-116.
DR PDB; 7ACJ; EM; 3.20 A; r=2-113.
DR PDB; 7ACR; EM; 3.44 A; r=2-113.
DR PDB; 7AF3; EM; 2.82 A; M=1-118.
DR PDB; 7AF5; EM; 2.96 A; M=1-118.
DR PDB; 7AF8; EM; 2.75 A; M=1-118.
DR PDB; 7AFA; EM; 2.95 A; M=1-118.
DR PDB; 7AFD; EM; 3.44 A; M=1-118.
DR PDB; 7AFH; EM; 3.59 A; M=1-118.
DR PDB; 7AFK; EM; 4.90 A; M=1-118.
DR PDB; 7AFN; EM; 3.86 A; M=1-118.
DR PDB; 7B5K; EM; 2.90 A; m=2-115.
DR PDB; 7BOE; EM; 2.90 A; M=1-118.
DR PDB; 7BOH; EM; 2.82 A; M=1-118.
DR PDB; 7D6Z; EM; 3.40 A; t=1-118.
DR PDB; 7D80; EM; 4.10 A; N=1-118.
DR PDB; 7JSS; EM; 3.70 A; R=2-115.
DR PDB; 7JSW; EM; 3.80 A; R=2-115.
DR PDB; 7JSZ; EM; 3.70 A; R=2-115.
DR PDB; 7JT1; EM; 3.30 A; R=2-115.
DR PDB; 7JT2; EM; 3.50 A; R=2-115.
DR PDB; 7JT3; EM; 3.70 A; R=2-115.
DR PDB; 7K50; EM; 3.40 A; R=2-115.
DR PDB; 7K51; EM; 3.50 A; R=2-115.
DR PDB; 7K52; EM; 3.40 A; R=2-115.
DR PDB; 7K53; EM; 3.20 A; R=2-115.
DR PDB; 7K54; EM; 3.20 A; R=2-115.
DR PDB; 7K55; EM; 3.30 A; R=2-115.
DR PDB; 7LV0; EM; 3.20 A; R=2-115.
DR PDB; 7N1P; EM; 2.33 A; SM=1-118.
DR PDB; 7N2C; EM; 2.72 A; SM=1-118.
DR PDB; 7N2U; EM; 2.53 A; SM=1-118.
DR PDB; 7N2V; EM; 2.54 A; SM=1-118.
DR PDB; 7N30; EM; 2.66 A; SM=1-118.
DR PDB; 7N31; EM; 2.69 A; SM=1-118.
DR PDB; 7NAR; EM; 3.00 A; M=1-118.
DR PDB; 7NAT; EM; 3.59 A; M=1-118.
DR PDB; 7NAU; EM; 3.78 A; M=1-118.
DR PDB; 7NAV; EM; 4.80 A; M=1-118.
DR PDB; 7NBU; EM; 3.11 A; M=2-116.
DR PDB; 7O19; EM; 2.90 A; AM=1-118.
DR PDB; 7O1A; EM; 2.40 A; AM=1-118.
DR PDB; 7O1C; EM; 2.60 A; AM=1-118.
DR PDB; 7OE0; EM; 2.69 A; M=2-118.
DR PDB; 7OE1; EM; 3.05 A; M=2-118.
DR PDB; 7OIZ; EM; 2.90 A; M=1-118.
DR PDB; 7OJ0; EM; 3.50 A; M=1-118.
DR PDB; 7P3K; EM; 2.90 A; M=1-118.
DR PDB; 7PJV; EM; 3.10 A; m=1-118.
DR PDB; 7PJY; EM; 3.10 A; m=1-118.
DR PDB; 7QG8; EM; 3.97 A; F=1-118.
DR PDB; 7QGH; EM; 4.48 A; D=1-118.
DR PDB; 7SS9; EM; 3.90 A; R=2-115.
DR PDB; 7SSD; EM; 3.30 A; R=2-115.
DR PDB; 7SSL; EM; 3.80 A; R=2-115.
DR PDB; 7SSN; EM; 3.20 A; R=2-115.
DR PDB; 7SSO; EM; 3.20 A; R=2-115.
DR PDB; 7SSW; EM; 3.80 A; R=2-115.
DR PDB; 7ST2; EM; 2.90 A; R=2-115.
DR PDB; 7ST6; EM; 3.00 A; R=2-115.
DR PDB; 7ST7; EM; 3.20 A; R=2-115.
DR PDBsum; 2YKR; -.
DR PDBsum; 3J9Y; -.
DR PDBsum; 3J9Z; -.
DR PDBsum; 3JA1; -.
DR PDBsum; 3JBU; -.
DR PDBsum; 3JBV; -.
DR PDBsum; 3JCD; -.
DR PDBsum; 3JCE; -.
DR PDBsum; 3JCJ; -.
DR PDBsum; 3JCN; -.
DR PDBsum; 4A2I; -.
DR PDBsum; 4ADV; -.
DR PDBsum; 4U1U; -.
DR PDBsum; 4U1V; -.
DR PDBsum; 4U20; -.
DR PDBsum; 4U24; -.
DR PDBsum; 4U25; -.
DR PDBsum; 4U26; -.
DR PDBsum; 4U27; -.
DR PDBsum; 4V47; -.
DR PDBsum; 4V48; -.
DR PDBsum; 4V4H; -.
DR PDBsum; 4V4Q; -.
DR PDBsum; 4V4V; -.
DR PDBsum; 4V4W; -.
DR PDBsum; 4V50; -.
DR PDBsum; 4V52; -.
DR PDBsum; 4V53; -.
DR PDBsum; 4V54; -.
DR PDBsum; 4V55; -.
DR PDBsum; 4V56; -.
DR PDBsum; 4V57; -.
DR PDBsum; 4V5B; -.
DR PDBsum; 4V5H; -.
DR PDBsum; 4V5Y; -.
DR PDBsum; 4V64; -.
DR PDBsum; 4V65; -.
DR PDBsum; 4V66; -.
DR PDBsum; 4V69; -.
DR PDBsum; 4V6C; -.
DR PDBsum; 4V6D; -.
DR PDBsum; 4V6E; -.
DR PDBsum; 4V6K; -.
DR PDBsum; 4V6L; -.
DR PDBsum; 4V6N; -.
DR PDBsum; 4V6O; -.
DR PDBsum; 4V6P; -.
DR PDBsum; 4V6Q; -.
DR PDBsum; 4V6R; -.
DR PDBsum; 4V6S; -.
DR PDBsum; 4V6T; -.
DR PDBsum; 4V6V; -.
DR PDBsum; 4V6Y; -.
DR PDBsum; 4V6Z; -.
DR PDBsum; 4V70; -.
DR PDBsum; 4V71; -.
DR PDBsum; 4V72; -.
DR PDBsum; 4V73; -.
DR PDBsum; 4V74; -.
DR PDBsum; 4V75; -.
DR PDBsum; 4V76; -.
DR PDBsum; 4V77; -.
DR PDBsum; 4V78; -.
DR PDBsum; 4V79; -.
DR PDBsum; 4V7A; -.
DR PDBsum; 4V7B; -.
DR PDBsum; 4V7C; -.
DR PDBsum; 4V7D; -.
DR PDBsum; 4V7I; -.
DR PDBsum; 4V7S; -.
DR PDBsum; 4V7T; -.
DR PDBsum; 4V7U; -.
DR PDBsum; 4V7V; -.
DR PDBsum; 4V85; -.
DR PDBsum; 4V89; -.
DR PDBsum; 4V9C; -.
DR PDBsum; 4V9D; -.
DR PDBsum; 4V9O; -.
DR PDBsum; 4V9P; -.
DR PDBsum; 4WF1; -.
DR PDBsum; 4WOI; -.
DR PDBsum; 4WWW; -.
DR PDBsum; 4YBB; -.
DR PDBsum; 5AFI; -.
DR PDBsum; 5H5U; -.
DR PDBsum; 5IQR; -.
DR PDBsum; 5IT8; -.
DR PDBsum; 5J5B; -.
DR PDBsum; 5J7L; -.
DR PDBsum; 5J88; -.
DR PDBsum; 5J8A; -.
DR PDBsum; 5J91; -.
DR PDBsum; 5JC9; -.
DR PDBsum; 5JTE; -.
DR PDBsum; 5JU8; -.
DR PDBsum; 5KCR; -.
DR PDBsum; 5KCS; -.
DR PDBsum; 5KPS; -.
DR PDBsum; 5KPV; -.
DR PDBsum; 5KPW; -.
DR PDBsum; 5KPX; -.
DR PDBsum; 5L3P; -.
DR PDBsum; 5LZA; -.
DR PDBsum; 5LZB; -.
DR PDBsum; 5LZC; -.
DR PDBsum; 5LZD; -.
DR PDBsum; 5LZE; -.
DR PDBsum; 5LZF; -.
DR PDBsum; 5MDV; -.
DR PDBsum; 5MDW; -.
DR PDBsum; 5MDY; -.
DR PDBsum; 5MDZ; -.
DR PDBsum; 5ME0; -.
DR PDBsum; 5ME1; -.
DR PDBsum; 5MGP; -.
DR PDBsum; 5MY1; -.
DR PDBsum; 5NO2; -.
DR PDBsum; 5NO3; -.
DR PDBsum; 5NO4; -.
DR PDBsum; 5NP6; -.
DR PDBsum; 5NWY; -.
DR PDBsum; 5O2R; -.
DR PDBsum; 5U4I; -.
DR PDBsum; 5U9F; -.
DR PDBsum; 5U9G; -.
DR PDBsum; 5UYK; -.
DR PDBsum; 5UYL; -.
DR PDBsum; 5UYM; -.
DR PDBsum; 5UYN; -.
DR PDBsum; 5UYP; -.
DR PDBsum; 5UYQ; -.
DR PDBsum; 5UZ4; -.
DR PDBsum; 5WDT; -.
DR PDBsum; 5WE4; -.
DR PDBsum; 5WE6; -.
DR PDBsum; 5WFK; -.
DR PDBsum; 6BU8; -.
DR PDBsum; 6BY1; -.
DR PDBsum; 6C4I; -.
DR PDBsum; 6DNC; -.
DR PDBsum; 6ENF; -.
DR PDBsum; 6ENJ; -.
DR PDBsum; 6ENU; -.
DR PDBsum; 6GWT; -.
DR PDBsum; 6GXM; -.
DR PDBsum; 6GXN; -.
DR PDBsum; 6GXO; -.
DR PDBsum; 6GXP; -.
DR PDBsum; 6H4N; -.
DR PDBsum; 6H58; -.
DR PDBsum; 6HRM; -.
DR PDBsum; 6I7V; -.
DR PDBsum; 6O9J; -.
DR PDBsum; 6O9K; -.
DR PDBsum; 6OFX; -.
DR PDBsum; 6OG7; -.
DR PDBsum; 6ORE; -.
DR PDBsum; 6ORL; -.
DR PDBsum; 6OST; -.
DR PDBsum; 6OT3; -.
DR PDBsum; 6OUO; -.
DR PDBsum; 6Q98; -.
DR PDBsum; 6Q9A; -.
DR PDBsum; 6SZS; -.
DR PDBsum; 6TBV; -.
DR PDBsum; 6TC3; -.
DR PDBsum; 6VWL; -.
DR PDBsum; 6VWM; -.
DR PDBsum; 6VWN; -.
DR PDBsum; 6W6K; -.
DR PDBsum; 6W77; -.
DR PDBsum; 6W7M; -.
DR PDBsum; 6W7N; -.
DR PDBsum; 6WD6; -.
DR PDBsum; 6WDB; -.
DR PDBsum; 6WDC; -.
DR PDBsum; 6WDD; -.
DR PDBsum; 6WDE; -.
DR PDBsum; 6WDF; -.
DR PDBsum; 6WDG; -.
DR PDBsum; 6WDH; -.
DR PDBsum; 6WDI; -.
DR PDBsum; 6WDJ; -.
DR PDBsum; 6WDK; -.
DR PDBsum; 6WDL; -.
DR PDBsum; 6WDM; -.
DR PDBsum; 6WNV; -.
DR PDBsum; 6WNW; -.
DR PDBsum; 6XE0; -.
DR PDBsum; 6XZA; -.
DR PDBsum; 6XZB; -.
DR PDBsum; 6Y69; -.
DR PDBsum; 6ZTL; -.
DR PDBsum; 7ABZ; -.
DR PDBsum; 7AC7; -.
DR PDBsum; 7ACJ; -.
DR PDBsum; 7ACR; -.
DR PDBsum; 7AF3; -.
DR PDBsum; 7AF5; -.
DR PDBsum; 7AF8; -.
DR PDBsum; 7AFA; -.
DR PDBsum; 7AFD; -.
DR PDBsum; 7AFH; -.
DR PDBsum; 7AFK; -.
DR PDBsum; 7AFN; -.
DR PDBsum; 7B5K; -.
DR PDBsum; 7BOE; -.
DR PDBsum; 7BOH; -.
DR PDBsum; 7D6Z; -.
DR PDBsum; 7D80; -.
DR PDBsum; 7JSS; -.
DR PDBsum; 7JSW; -.
DR PDBsum; 7JSZ; -.
DR PDBsum; 7JT1; -.
DR PDBsum; 7JT2; -.
DR PDBsum; 7JT3; -.
DR PDBsum; 7K50; -.
DR PDBsum; 7K51; -.
DR PDBsum; 7K52; -.
DR PDBsum; 7K53; -.
DR PDBsum; 7K54; -.
DR PDBsum; 7K55; -.
DR PDBsum; 7LV0; -.
DR PDBsum; 7N1P; -.
DR PDBsum; 7N2C; -.
DR PDBsum; 7N2U; -.
DR PDBsum; 7N2V; -.
DR PDBsum; 7N30; -.
DR PDBsum; 7N31; -.
DR PDBsum; 7NAR; -.
DR PDBsum; 7NAT; -.
DR PDBsum; 7NAU; -.
DR PDBsum; 7NAV; -.
DR PDBsum; 7NBU; -.
DR PDBsum; 7O19; -.
DR PDBsum; 7O1A; -.
DR PDBsum; 7O1C; -.
DR PDBsum; 7OE0; -.
DR PDBsum; 7OE1; -.
DR PDBsum; 7OIZ; -.
DR PDBsum; 7OJ0; -.
DR PDBsum; 7P3K; -.
DR PDBsum; 7PJV; -.
DR PDBsum; 7PJY; -.
DR PDBsum; 7QG8; -.
DR PDBsum; 7QGH; -.
DR PDBsum; 7SS9; -.
DR PDBsum; 7SSD; -.
DR PDBsum; 7SSL; -.
DR PDBsum; 7SSN; -.
DR PDBsum; 7SSO; -.
DR PDBsum; 7SSW; -.
DR PDBsum; 7ST2; -.
DR PDBsum; 7ST6; -.
DR PDBsum; 7ST7; -.
DR AlphaFoldDB; P0A7S9; -.
DR SMR; P0A7S9; -.
DR ComplexPortal; CPX-3802; 30S small ribosomal subunit.
DR DIP; DIP-35855N; -.
DR IntAct; P0A7S9; 119.
DR STRING; 511145.b3298; -.
DR DrugBank; DB00560; Tigecycline.
DR jPOST; P0A7S9; -.
DR PaxDb; P0A7S9; -.
DR PRIDE; P0A7S9; -.
DR EnsemblBacteria; AAC76323; AAC76323; b3298.
DR EnsemblBacteria; BAE77993; BAE77993; BAE77993.
DR GeneID; 67415339; -.
DR GeneID; 947791; -.
DR KEGG; ecj:JW3260; -.
DR KEGG; eco:b3298; -.
DR PATRIC; fig|1411691.4.peg.3433; -.
DR EchoBASE; EB0905; -.
DR eggNOG; COG0099; Bacteria.
DR HOGENOM; CLU_103849_1_2_6; -.
DR InParanoid; P0A7S9; -.
DR OMA; YRGLRHK; -.
DR PhylomeDB; P0A7S9; -.
DR BioCyc; EcoCyc:EG10912-MON; -.
DR BioCyc; MetaCyc:EG10912-MON; -.
DR EvolutionaryTrace; P0A7S9; -.
DR PRO; PR:P0A7S9; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:EcoliWiki.
DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0002181; P:cytoplasmic translation; IC:ComplexPortal.
DR Gene3D; 4.10.910.10; -; 1.
DR HAMAP; MF_01315; Ribosomal_S13_S18; 1.
DR InterPro; IPR027437; 30s_Rbsml_prot_S13_C.
DR InterPro; IPR001892; Ribosomal_S13.
DR InterPro; IPR010979; Ribosomal_S13-like_H2TH.
DR InterPro; IPR019980; Ribosomal_S13_bac-type.
DR InterPro; IPR018269; Ribosomal_S13_CS.
DR PANTHER; PTHR10871:SF1; PTHR10871:SF1; 1.
DR Pfam; PF00416; Ribosomal_S13; 1.
DR PIRSF; PIRSF002134; Ribosomal_S13; 1.
DR SUPFAM; SSF46946; SSF46946; 1.
DR TIGRFAMs; TIGR03631; uS13_bact; 1.
DR PROSITE; PS00646; RIBOSOMAL_S13_1; 1.
DR PROSITE; PS50159; RIBOSOMAL_S13_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding;
KW tRNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:330375"
FT CHAIN 2..118
FT /note="30S ribosomal protein S13"
FT /id="PRO_0000132089"
FT REGION 94..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 89..99
FT /note="Missing (in PW118; partially suppresses a rimM
FT deletion)"
FT /evidence="ECO:0000269|PubMed:9226267"
FT VARIANT 100..118
FT /note="Missing (in rpsM413; pseudorevertant of streptomycin
FT resistance. A strong antisuppressor of two tRNA
FT suppressors, decreases translation step time and growth
FT rate)"
FT /evidence="ECO:0000269|PubMed:8193163"
FT VARIANT 105
FT /note="N -> H (in PW095; partially suppresses a rimM
FT deletion)"
FT /evidence="ECO:0000269|PubMed:9226267"
FT VARIANT 105
FT /note="N -> K (in PW097; partially suppresses a rimM
FT deletion)"
FT /evidence="ECO:0000269|PubMed:9226267"
FT MUTAGEN 83..118
FT /note="Missing: Decreased growth rate at all temperatures.
FT Decreased affinity of the 30S subunit P site for tRNA in
FT vitro."
FT /evidence="ECO:0000269|PubMed:15308780"
FT MUTAGEN 114..118
FT /note="Missing: Decreased growth rate at all temperatures.
FT Decreased affinity of the 30S subunit P site for tRNA in
FT vitro."
FT /evidence="ECO:0000269|PubMed:15308780"
FT STRAND 4..7
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 12..14
FT /evidence="ECO:0007829|PDB:7BOH"
FT HELIX 18..21
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 23..25
FT /evidence="ECO:0007829|PDB:7OE0"
FT TURN 27..31
FT /evidence="ECO:0007829|PDB:7OE0"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:7OE1"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:7OE0"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:7OE0"
FT HELIX 66..79
FT /evidence="ECO:0007829|PDB:7OE0"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:7OE0"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:7OE0"
FT TURN 91..94
FT /evidence="ECO:0007829|PDB:7OE0"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:7BOH"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:7OE0"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:7OE0"
SQ SEQUENCE 118 AA; 13099 MW; 6277C365EBE4F732 CRC64;
MARIAGINIP DHKHAVIALT SIYGVGKTRS KAILAAAGIA EDVKISELSE GQIDTLRDEV
AKFVVEGDLR REISMSIKRL MDLGCYRGLR HRRGLPVRGQ RTKTNARTRK GPRKPIKK
