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TOLB_ECOLI
ID   TOLB_ECOLI              Reviewed;         430 AA.
AC   P0A855; P19935;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2005, sequence version 1.
DT   03-AUG-2022, entry version 140.
DE   RecName: Full=Tol-Pal system protein TolB {ECO:0000255|HAMAP-Rule:MF_00671, ECO:0000305};
DE   Flags: Precursor;
GN   Name=tolB {ECO:0000255|HAMAP-Rule:MF_00671, ECO:0000303|PubMed:2687247};
GN   OrderedLocusNames=b0740, JW5100;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=K12 / JM105 / ATCC 47016;
RX   PubMed=2687247; DOI=10.1128/jb.171.12.6600-6609.1989;
RA   Levengood S.K., Webster R.E.;
RT   "Nucleotide sequences of the tolA and tolB genes and localization of their
RT   products, components of a multistep translocation system in Escherichia
RT   coli.";
RL   J. Bacteriol. 171:6600-6609(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [3]
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   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 419-430.
RC   STRAIN=K12;
RX   PubMed=1574003; DOI=10.1111/j.1365-2958.1992.tb01523.x;
RA   Lazzaroni J.-C., Portalier R.;
RT   "The excC gene of Escherichia coli K-12 required for cell envelope
RT   integrity encodes the peptidoglycan-associated lipoprotein (PAL).";
RL   Mol. Microbiol. 6:735-742(1992).
RN   [6]
RP   PROTEIN SEQUENCE OF 22-27, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=7929011; DOI=10.1128/jb.176.20.6392-6396.1994;
RA   Isnard M., Rigal A., Lazzaroni J.-C., Lazdunski C., Lloubes R.;
RT   "Maturation and localization of the TolB protein required for colicin
RT   import.";
RL   J. Bacteriol. 176:6392-6396(1994).
RN   [7]
RP   PROTEIN SEQUENCE OF 22-32.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA   Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
RL   Submitted (FEB-1996) to UniProtKB.
RN   [8]
RP   INTERACTION WITH PAL, AND SUBCELLULAR LOCATION.
RX   PubMed=7744736; DOI=10.1074/jbc.270.19.11071;
RA   Bouveret E., Derouiche R., Rigal A., Lloubes R., Lazdunski C.,
RA   Benedetti H.;
RT   "Peptidoglycan-associated lipoprotein-TolB interaction. A possible key to
RT   explaining the formation of contact sites between the inner and outer
RT   membranes of Escherichia coli.";
RL   J. Biol. Chem. 270:11071-11077(1995).
RN   [9]
RP   INTERACTION WITH PORINS.
RX   PubMed=9393690; DOI=10.1128/jb.179.23.7274-7279.1997;
RA   Rigal A., Bouveret E., Lloubes R., Lazdunski C., Benedetti H.;
RT   "The TolB protein interacts with the porins of Escherichia coli.";
RL   J. Bacteriol. 179:7274-7279(1997).
RN   [10]
RP   INTERACTION WITH PAL; LPP AND OMPA.
RX   PubMed=9701827; DOI=10.1046/j.1365-2958.1998.00945.x;
RA   Clavel T., Germon P., Vianney A., Portalier R., Lazzaroni J.-C.;
RT   "TolB protein of Escherichia coli K-12 interacts with the outer membrane
RT   peptidoglycan-associated proteins Pal, Lpp and OmpA.";
RL   Mol. Microbiol. 29:359-367(1998).
RN   [11]
RP   FUNCTION, SUBUNIT, AND INTERACTION WITH TOLA.
RX   PubMed=11994151; DOI=10.1046/j.1365-2958.2002.02895.x;
RA   Walburger A., Lazdunski C., Corda Y.;
RT   "The Tol/Pal system function requires an interaction between the C-terminal
RT   domain of TolA and the N-terminal domain of TolB.";
RL   Mol. Microbiol. 44:695-708(2002).
RN   [12]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=17233825; DOI=10.1111/j.1365-2958.2006.05571.x;
RA   Gerding M.A., Ogata Y., Pecora N.D., Niki H., de Boer P.A.;
RT   "The trans-envelope Tol-Pal complex is part of the cell division machinery
RT   and required for proper outer-membrane invagination during cell
RT   constriction in E. coli.";
RL   Mol. Microbiol. 63:1008-1025(2007).
RN   [13]
RP   FUNCTION.
RX   PubMed=24720726; DOI=10.1111/mmi.12609;
RA   Santos T.M., Lin T.Y., Rajendran M., Anderson S.M., Weibel D.B.;
RT   "Polar localization of Escherichia coli chemoreceptors requires an intact
RT   Tol-Pal complex.";
RL   Mol. Microbiol. 92:985-1004(2014).
RN   [14]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=32152098; DOI=10.1073/pnas.1919267117;
RA   Yakhnina A.A., Bernhardt T.G.;
RT   "The Tol-Pal system is required for peptidoglycan-cleaving enzymes to
RT   complete bacterial cell division.";
RL   Proc. Natl. Acad. Sci. U.S.A. 117:6777-6783(2020).
RN   [15]
RP   CRYSTALLIZATION.
RX   PubMed=9761825; DOI=10.1107/s0907444997008020;
RA   Abergel C., Rigal A., Chenivesse S., Lazdunski C., Claverie J.-M.,
RA   Bouveret E., Benedetti H.;
RT   "Crystallization and preliminary crystallographic study of a component of
RT   the Escherichia coli Tol system: TolB.";
RL   Acta Crystallogr. D 54:102-104(1998).
RN   [16] {ECO:0007744|PDB:1CRZ}
RP   X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RX   PubMed=10545334; DOI=10.1016/s0969-2126(00)80062-3;
RA   Abergel C., Bouveret E., Claverie J.-M., Brown K., Rigal A., Lazdunski C.,
RA   Benedetti H.;
RT   "Structure of the Escherichia coli TolB protein determined by MAD methods
RT   at 1.95-A resolution.";
RL   Structure 7:1291-1300(1999).
RN   [17] {ECO:0007744|PDB:1C5K}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), AND INTERACTION WITH COLICIN E9.
RX   PubMed=10673426; DOI=10.1016/s0969-2126(00)00079-4;
RA   Carr S., Penfold C.N., Bamford V., James R., Hemmings A.M.;
RT   "The structure of TolB, an essential component of the tol-dependent
RT   translocation system, and its protein-protein interaction with the
RT   translocation domain of colicin E9.";
RL   Structure 8:57-66(2000).
RN   [18] {ECO:0007744|PDB:2IVZ}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH COLICIN E9.
RX   PubMed=16894158; DOI=10.1073/pnas.0603433103;
RA   Loftus S.R., Walker D., Mate M.J., Bonsor D.A., James R., Moore G.R.,
RA   Kleanthous C.;
RT   "Competitive recruitment of the periplasmic translocation portal TolB by a
RT   natively disordered domain of colicin E9.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:12353-12358(2006).
RN   [19] {ECO:0007744|PDB:2HQS}
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 23-430 IN COMPLEX WITH PAL.
RX   PubMed=17375930; DOI=10.1021/ja070153n;
RA   Bonsor D.A., Grishkovskaya I., Dodson E.J., Kleanthous C.;
RT   "Molecular mimicry enables competitive recruitment by a natively disordered
RT   protein.";
RL   J. Am. Chem. Soc. 129:4800-4807(2007).
RN   [20] {ECO:0007744|PDB:2W8B}
RP   X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 22-430 IN COMPLEX WITH PAL,
RP   FUNCTION, AND DOMAIN.
RX   PubMed=19696740; DOI=10.1038/emboj.2009.224;
RA   Bonsor D.A., Hecht O., Vankemmelbeke M., Sharma A., Krachler A.M.,
RA   Housden N.G., Lilly K.J., James R., Moore G.R., Kleanthous C.;
RT   "Allosteric beta-propeller signalling in TolB and its manipulation by
RT   translocating colicins.";
RL   EMBO J. 28:2846-2857(2009).
CC   -!- FUNCTION: Part of the Tol-Pal system, which plays a role in outer
CC       membrane invagination during cell division and is important for
CC       maintaining outer membrane integrity (PubMed:17233825). TolB occupies a
CC       key intermediary position in the Tol-Pal system because it communicates
CC       directly with both membrane-embedded components, Pal in the outer
CC       membrane and TolA in the inner membrane (PubMed:19696740). The Tol-Pal
CC       system is also required for polar localization of chemoreceptors
CC       clusters (PubMed:24720726). The system also appears to be required for
CC       the activity of several outer membrane-localized enzymes with cell wall
CC       remodeling activity (PubMed:32152098). Is involved in the uptake of
CC       some colicins A (PubMed:2687247, PubMed:7929011, PubMed:11994151).
CC       {ECO:0000269|PubMed:11994151, ECO:0000269|PubMed:17233825,
CC       ECO:0000269|PubMed:19696740, ECO:0000269|PubMed:24720726,
CC       ECO:0000269|PubMed:32152098, ECO:0000305|PubMed:2687247,
CC       ECO:0000305|PubMed:7929011}.
CC   -!- SUBUNIT: The Tol-Pal system is composed of five core proteins: the
CC       inner membrane proteins TolA, TolQ and TolR, the periplasmic protein
CC       TolB and the outer membrane protein Pal. They form a network linking
CC       the inner and outer membranes and the peptidoglycan layer
CC       (PubMed:17233825). TolB forms homodimers (PubMed:11994151). Interacts
CC       with the peptidoglycan-associated lipoprotein Pal and with the C-
CC       terminal region of TolA (PubMed:7744736, PubMed:11994151,
CC       PubMed:17375930, PubMed:19696740). Interacts with the trimeric porins
CC       OmpF, OmpC, PhoE and LamB (PubMed:9393690). Can form a complex with
CC       Pal, Lpp and OmpA (PubMed:9701827). Interacts with colicin E9
CC       (PubMed:10673426, PubMed:16894158). {ECO:0000269|PubMed:10673426,
CC       ECO:0000269|PubMed:11994151, ECO:0000269|PubMed:16894158,
CC       ECO:0000269|PubMed:17375930, ECO:0000269|PubMed:19696740,
CC       ECO:0000269|PubMed:7744736, ECO:0000269|PubMed:9393690,
CC       ECO:0000269|PubMed:9701827, ECO:0000305|PubMed:17233825}.
CC   -!- INTERACTION:
CC       P0A855; P0A912: pal; NbExp=4; IntAct=EBI-7180728, EBI-1124760;
CC       P0A855; P19934: tolA; NbExp=5; IntAct=EBI-7180728, EBI-1120026;
CC       P0A855; P09883: col; Xeno; NbExp=9; IntAct=EBI-7180728, EBI-1029888;
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00671,
CC       ECO:0000269|PubMed:2687247, ECO:0000269|PubMed:7929011}. Note=Partially
CC       associated with the outer membrane through a specific interaction with
CC       Pal (PubMed:7744736). Accumulates at cell constriction sites.
CC       Recruitment to the division site is dependent on FtsN activity
CC       (PubMed:17233825). {ECO:0000269|PubMed:17233825,
CC       ECO:0000269|PubMed:7744736}.
CC   -!- DOMAIN: Effector proteins that bind to TolB can both negatively (Pal)
CC       and positively (colicin E9) regulate association of the distal N-
CC       terminal TolA box with TolA by influencing the conformational
CC       equilibrium experienced by these residues.
CC       {ECO:0000269|PubMed:19696740}.
CC   -!- DISRUPTION PHENOTYPE: Mutants lacking the tol-pal cluster suffer
CC       delayed outer membrane invagination and contain large outer membrane
CC       blebs at constriction sites and cell poles (PubMed:17233825). Tol-pal
CC       mutants fail to complete division and form cell chains, and fail to
CC       process denuded peptidoglycans at the septum (PubMed:32152098).
CC       {ECO:0000269|PubMed:17233825, ECO:0000269|PubMed:32152098}.
CC   -!- SIMILARITY: Belongs to the TolB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00671, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA24684.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M28232; AAA24684.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC73834.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35406.2; -; Genomic_DNA.
DR   EMBL; X65796; CAA46672.1; -; Genomic_DNA.
DR   PIR; C64810; C64810.
DR   RefSeq; NP_415268.1; NC_000913.3.
DR   RefSeq; WP_001295307.1; NZ_STEB01000035.1.
DR   PDB; 1C5K; X-ray; 2.00 A; A=1-430.
DR   PDB; 1CRZ; X-ray; 1.95 A; A=28-430.
DR   PDB; 2HQS; X-ray; 1.50 A; A/B/D/F=23-430.
DR   PDB; 2IVZ; X-ray; 2.00 A; A/B/C/D=1-430.
DR   PDB; 2W8B; X-ray; 1.86 A; A/B/D/F=22-430.
DR   PDB; 3IAX; X-ray; 2.60 A; A=1-430.
DR   PDB; 7NST; EM; 3.70 A; E=1-430.
DR   PDB; 7NSU; EM; 4.70 A; E=1-430.
DR   PDBsum; 1C5K; -.
DR   PDBsum; 1CRZ; -.
DR   PDBsum; 2HQS; -.
DR   PDBsum; 2IVZ; -.
DR   PDBsum; 2W8B; -.
DR   PDBsum; 3IAX; -.
DR   PDBsum; 7NST; -.
DR   PDBsum; 7NSU; -.
DR   AlphaFoldDB; P0A855; -.
DR   SMR; P0A855; -.
DR   BioGRID; 4261828; 397.
DR   BioGRID; 849803; 7.
DR   ComplexPortal; CPX-5782; Tol-Pal cell envelope complex.
DR   DIP; DIP-48262N; -.
DR   IntAct; P0A855; 11.
DR   MINT; P0A855; -.
DR   STRING; 511145.b0740; -.
DR   TCDB; 2.C.1.2.1; the tonb-exbb-exbd/tola-tolq-tolr outer membrane receptor energizers and stabilizers (tonb/tola) family.
DR   SWISS-2DPAGE; P0A855; -.
DR   jPOST; P0A855; -.
DR   PaxDb; P0A855; -.
DR   PRIDE; P0A855; -.
DR   EnsemblBacteria; AAC73834; AAC73834; b0740.
DR   EnsemblBacteria; BAA35406; BAA35406; BAA35406.
DR   GeneID; 66670990; -.
DR   GeneID; 945429; -.
DR   KEGG; ecj:JW5100; -.
DR   KEGG; eco:b0740; -.
DR   PATRIC; fig|1411691.4.peg.1532; -.
DR   EchoBASE; EB1001; -.
DR   eggNOG; COG0823; Bacteria.
DR   HOGENOM; CLU_047123_0_0_6; -.
DR   InParanoid; P0A855; -.
DR   OMA; VREPSWG; -.
DR   PhylomeDB; P0A855; -.
DR   BioCyc; EcoCyc:EG11008-MON; -.
DR   BioCyc; MetaCyc:EG11008-MON; -.
DR   EvolutionaryTrace; P0A855; -.
DR   PRO; PR:P0A855; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0032153; C:cell division site; IDA:EcoCyc.
DR   GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR   GO; GO:0042597; C:periplasmic space; IDA:EcoliWiki.
DR   GO; GO:0032991; C:protein-containing complex; IDA:CAFA.
DR   GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:CAFA.
DR   GO; GO:0043213; P:bacteriocin transport; IMP:EcoliWiki.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IC:ComplexPortal.
DR   GO; GO:0071237; P:cellular response to bacteriocin; IDA:EcoCyc.
DR   GO; GO:0017038; P:protein import; IMP:EcoliWiki.
DR   GO; GO:0015031; P:protein transport; IMP:EcoliWiki.
DR   GO; GO:1905153; P:regulation of membrane invagination; IC:ComplexPortal.
DR   Gene3D; 2.120.10.30; -; 1.
DR   HAMAP; MF_00671; TolB; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR011659; PD40.
DR   InterPro; IPR014167; Tol-Pal_TolB.
DR   InterPro; IPR007195; TolB_N.
DR   Pfam; PF07676; PD40; 4.
DR   Pfam; PF04052; TolB_N; 1.
DR   TIGRFAMs; TIGR02800; propeller_TolB; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Direct protein sequencing;
KW   Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00671,
FT                   ECO:0000269|PubMed:7929011, ECO:0000269|Ref.7"
FT   CHAIN           22..430
FT                   /note="Tol-Pal system protein TolB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00671"
FT                   /id="PRO_0000034647"
FT   REGION          22..34
FT                   /note="TolA box"
FT                   /evidence="ECO:0000305|PubMed:19696740"
FT   STRAND          26..29
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          31..33
FT                   /evidence="ECO:0007829|PDB:1CRZ"
FT   STRAND          34..39
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          43..49
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   HELIX           54..64
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          67..70
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   HELIX           73..75
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   HELIX           83..85
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   HELIX           88..92
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   TURN            93..95
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          98..106
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          112..120
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          122..124
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          128..136
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   HELIX           138..140
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   HELIX           141..157
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          166..172
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          174..177
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          180..186
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          193..200
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          202..207
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          211..218
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          225..230
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   TURN            231..233
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          236..240
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          246..251
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          255..262
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          269..274
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   TURN            275..277
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          280..282
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          286..288
FT                   /evidence="ECO:0007829|PDB:1CRZ"
FT   STRAND          290..295
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          299..306
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          313..318
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          330..339
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          343..351
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          356..362
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   TURN            363..365
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          368..370
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          374..376
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          378..382
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          386..395
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          398..405
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          411..413
FT                   /evidence="ECO:0007829|PDB:2HQS"
FT   STRAND          417..426
FT                   /evidence="ECO:0007829|PDB:2HQS"
SQ   SEQUENCE   430 AA;  45956 MW;  508795C6E6886B52 CRC64;
     MKQALRVAFG FLILWASVLH AEVRIVIDSG VDSGRPIGVV PFQWAGPGAA PEDIGGIVAA
     DLRNSGKFNP LDRARLPQQP GSAQEVQPAA WSALGIDAVV VGQVTPNPDG SYNVAYQLVD
     TGGAPGTVLA QNSYKVNKQW LRYAGHTASD EVFEKLTGIK GAFRTRIAYV VQTNGGQFPY
     ELRVSDYDGY NQFVVHRSPQ PLMSPAWSPD GSKLAYVTFE SGRSALVIQT LANGAVRQVA
     SFPRHNGAPA FSPDGSKLAF ALSKTGSLNL YVMDLASGQI RQVTDGRSNN TEPTWFPDSQ
     NLAFTSDQAG RPQVYKVNIN GGAPQRITWE GSQNQDADVS SDGKFMVMVS SNGGQQHIAK
     QDLATGGVQV LSSTFLDETP SLAPNGTMVI YSSSQGMGSV LNLVSTDGRF KARLPATDGQ
     VKFPAWSPYL
 
 
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