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SECB_ECOUT
ID   SECB_ECOUT              Reviewed;         155 AA.
AC   Q1R4Y5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Protein-export protein SecB {ECO:0000255|HAMAP-Rule:MF_00821};
GN   Name=secB {ECO:0000255|HAMAP-Rule:MF_00821}; OrderedLocusNames=UTI89_C4151;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
CC   -!- FUNCTION: One of the proteins required for the normal export of
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. It also specifically binds to its
CC       receptor SecA. {ECO:0000255|HAMAP-Rule:MF_00821}.
CC   -!- SUBUNIT: Homotetramer, a dimer of dimers. One homotetramer interacts
CC       with 1 SecA dimer. {ECO:0000255|HAMAP-Rule:MF_00821}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00821}.
CC   -!- SIMILARITY: Belongs to the SecB family. {ECO:0000255|HAMAP-
CC       Rule:MF_00821}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABE09579.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000243; ABE09579.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000003382.1; NC_007946.1.
DR   AlphaFoldDB; Q1R4Y5; -.
DR   SMR; Q1R4Y5; -.
DR   EnsemblBacteria; ABE09579; ABE09579; UTI89_C4151.
DR   GeneID; 66672493; -.
DR   KEGG; eci:UTI89_C4151; -.
DR   HOGENOM; CLU_111574_1_0_6; -.
DR   OMA; CPNVLFP; -.
DR   Proteomes; UP000001952; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
DR   GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Protein transport; Translocation; Transport.
FT   CHAIN           1..155
FT                   /note="Protein-export protein SecB"
FT                   /id="PRO_0000318224"
SQ   SEQUENCE   155 AA;  17291 MW;  F5041AEF548CBF50 CRC64;
     MSEQNNTEMT FQIQRIYTKD ISFEAPNAPH VFQKDWQPEV KLDLDTASTQ LADDVYEVVL
     RVTVTASLGE ETAFLCEVQQ GGIFSIAGIE GTQMAHCLGA YCPNILFPYA RECITSMVSR
     GTFPQLNLAP VNFDALFMNY LQQQAGEGTE EHQDA
 
 
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