SECB_ECOLI
ID SECB_ECOLI Reviewed; 155 AA.
AC P0AG86; P15040; Q2M7S3;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 129.
DE RecName: Full=Protein-export protein SecB;
DE AltName: Full=Chaperone SecB;
GN Name=secB; OrderedLocusNames=b3609, JW3584;
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=2656409; DOI=10.1016/0378-1119(89)90393-4;
RA Kumamoto C.A., Nault A.K.;
RT "Characterization of the Escherichia coli protein-export gene secB.";
RL Gene 75:167-175(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8041620; DOI=10.1093/nar/22.13.2576;
RA Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.;
RT "Analysis of the Escherichia coli genome. V. DNA sequence of the region
RT from 76.0 to 81.5 minutes.";
RL Nucleic Acids Res. 22:2576-2586(1994).
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 IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [6]
RP FUNCTION, SUBSTRATES, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=16352602; DOI=10.1074/jbc.m509929200;
RA Baars L., Ytterberg A.J., Drew D., Wagner S., Thilo C., van Wijk K.J.,
RA de Gier J.W.;
RT "Defining the role of the Escherichia coli chaperone SecB using comparative
RT proteomics.";
RL J. Biol. Chem. 281:10024-10034(2006).
RN [7]
RP FUNCTION, SUBSTRATES, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=16522795; DOI=10.1110/ps.051889506;
RA Marani P., Wagner S., Baars L., Genevaux P., de Gier J.W., Nilsson I.,
RA Casadio R., von Heijne G.;
RT "New Escherichia coli outer membrane proteins identified through prediction
RT and experimental verification.";
RL Protein Sci. 15:884-889(2006).
RN [8] {ECO:0007744|PDB:1QYN}
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-153, AND SUBUNIT.
RX PubMed=14643199; DOI=10.1016/j.jsb.2003.09.012;
RA Dekker C., de Kruijff B., Gros P.;
RT "Crystal structure of SecB from Escherichia coli.";
RL J. Struct. Biol. 144:313-319(2003).
RN [9] {ECO:0007744|PDB:5JTL, ECO:0007744|PDB:5JTM, ECO:0007744|PDB:5JTN, ECO:0007744|PDB:5JTO, ECO:0007744|PDB:5JTP, ECO:0007744|PDB:5JTQ, ECO:0007744|PDB:5JTR}
RP STRUCTURE BY NMR IN COMPLEX WITH SUBSTRATES, FUNCTION, AND SUBUNIT.
RX PubMed=27501151; DOI=10.1038/nature18965;
RA Huang C., Rossi P., Saio T., Kalodimos C.G.;
RT "Structural basis for the antifolding activity of a molecular chaperone.";
RL Nature 537:202-206(2016).
RN [10]
RP REVIEW OF PROTEIN SECRETION.
RX PubMed=17938627; DOI=10.1038/nrmicro1771;
RA Papanikou E., Karamanou S., Economou A.;
RT "Bacterial protein secretion through the translocase nanomachine.";
RL Nat. Rev. Microbiol. 5:839-851(2007).
CC -!- FUNCTION: One of the proteins required for the normal export of some
CC preproteins out of the cell cytoplasm. It is a molecular chaperone that
CC binds to a subset of precursor proteins, maintaining them in a
CC translocation-competent state. For 2 proteins (MBP, MalE and PhoA) the
CC substrate is wrapped around the homotetramer, which prevents it from
CC folding (PubMed:27501151). It also specifically binds to its receptor
CC SecA. Its substrates include DegP, FhuA, FkpA, GBP, LamB, MalE (MBP),
CC OmpA, OmpF, OmpT, OmpX, OppA, PhoE, TolB, TolC, YbgF, YcgK, YgiW and
CC YncE (PubMed:16352602). {ECO:0000269|PubMed:16352602,
CC ECO:0000269|PubMed:16522795, ECO:0000269|PubMed:27501151}.
CC -!- SUBUNIT: Homotetramer, a dimer of dimers (PubMed:14643199,
CC PubMed:27501151). One homotetramer interacts with 1 SecA dimer.
CC {ECO:0000269|PubMed:14643199, ECO:0000269|PubMed:27501151}.
CC -!- INTERACTION:
CC P0AG86; P0AE88: cpxR; NbExp=3; IntAct=EBI-555877, EBI-550918;
CC P0AG86; P10408: secA; NbExp=6; IntAct=EBI-555877, EBI-543213;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- DISRUPTION PHENOTYPE: Growth continues, but export of its substrates is
CC blocked (PubMed:16352602, PubMed:16522795). Expression of chaperones
CC DnaK, GroEL/ES, ClpB, and HslU increases (PubMed:16352602).
CC {ECO:0000269|PubMed:16352602, ECO:0000269|PubMed:16522795}.
CC -!- SIMILARITY: Belongs to the SecB family. {ECO:0000305}.
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DR EMBL; M24489; AAA83907.1; -; Genomic_DNA.
DR EMBL; U00039; AAB18586.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76633.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77683.1; -; Genomic_DNA.
DR PIR; JS0126; VXECS.
DR RefSeq; NP_418066.1; NC_000913.3.
DR RefSeq; WP_000003377.1; NZ_STEB01000024.1.
DR PDB; 1QYN; X-ray; 2.35 A; A/B/C/D=1-153.
DR PDB; 5JTL; NMR; -; A/B/C/D=1-155.
DR PDB; 5JTM; NMR; -; A/B/C/D=1-155.
DR PDB; 5JTN; NMR; -; A/B/C/D=1-155.
DR PDB; 5JTO; NMR; -; A/B/C/D=1-155.
DR PDB; 5JTP; NMR; -; A/B/C/D=1-155.
DR PDB; 5JTQ; NMR; -; A/B/C/D=1-155.
DR PDB; 5JTR; NMR; -; A/B/C/D=1-155.
DR PDBsum; 1QYN; -.
DR PDBsum; 5JTL; -.
DR PDBsum; 5JTM; -.
DR PDBsum; 5JTN; -.
DR PDBsum; 5JTO; -.
DR PDBsum; 5JTP; -.
DR PDBsum; 5JTQ; -.
DR PDBsum; 5JTR; -.
DR AlphaFoldDB; P0AG86; -.
DR SMR; P0AG86; -.
DR BioGRID; 4261403; 384.
DR DIP; DIP-47924N; -.
DR IntAct; P0AG86; 14.
DR STRING; 511145.b3609; -.
DR jPOST; P0AG86; -.
DR PaxDb; P0AG86; -.
DR PRIDE; P0AG86; -.
DR EnsemblBacteria; AAC76633; AAC76633; b3609.
DR EnsemblBacteria; BAE77683; BAE77683; BAE77683.
DR GeneID; 67417612; -.
DR GeneID; 948123; -.
DR KEGG; ecj:JW3584; -.
DR KEGG; eco:b3609; -.
DR PATRIC; fig|1411691.4.peg.3097; -.
DR EchoBASE; EB0930; -.
DR eggNOG; COG1952; Bacteria.
DR HOGENOM; CLU_111574_1_0_6; -.
DR InParanoid; P0AG86; -.
DR OMA; CPNVLFP; -.
DR PhylomeDB; P0AG86; -.
DR BioCyc; EcoCyc:SECB; -.
DR EvolutionaryTrace; P0AG86; -.
DR PRO; PR:P0AG86; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0070678; F:preprotein binding; IDA:EcoCyc.
DR GO; GO:0051082; F:unfolded protein binding; IDA:EcoCyc.
DR GO; GO:0036506; P:maintenance of unfolded protein; IDA:EcoCyc.
DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR GO; GO:0008104; P:protein localization; IMP:EcoCyc.
DR GO; GO:0006605; P:protein targeting; IMP:EcoliWiki.
DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IMP:EcoliWiki.
DR GO; GO:0043952; P:protein transport by the Sec complex; IMP:EcoliWiki.
DR Gene3D; 3.10.420.10; -; 1.
DR HAMAP; MF_00821; SecB; 1.
DR InterPro; IPR003708; SecB.
DR InterPro; IPR035958; SecB-like_sf.
DR PANTHER; PTHR36918; PTHR36918; 1.
DR Pfam; PF02556; SecB; 1.
DR PRINTS; PR01594; SECBCHAPRONE.
DR SUPFAM; SSF54611; SSF54611; 1.
DR TIGRFAMs; TIGR00809; secB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Protein transport; Reference proteome;
KW Translocation; Transport.
FT CHAIN 1..155
FT /note="Protein-export protein SecB"
FT /id="PRO_0000055370"
FT STRAND 4..6
FT /evidence="ECO:0007829|PDB:5JTM"
FT STRAND 10..24
FT /evidence="ECO:0007829|PDB:1QYN"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:1QYN"
FT STRAND 39..52
FT /evidence="ECO:0007829|PDB:1QYN"
FT STRAND 55..68
FT /evidence="ECO:0007829|PDB:1QYN"
FT STRAND 71..88
FT /evidence="ECO:0007829|PDB:1QYN"
FT HELIX 91..99
FT /evidence="ECO:0007829|PDB:1QYN"
FT HELIX 101..121
FT /evidence="ECO:0007829|PDB:1QYN"
FT HELIX 133..141
FT /evidence="ECO:0007829|PDB:1QYN"
SQ SEQUENCE 155 AA; 17277 MW; 00514C5F393A643D CRC64;
MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASSQ LADDVYEVVL
RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR
GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA
