SECB_VIBCH
ID SECB_VIBCH Reviewed; 154 AA.
AC Q9KNS8;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Protein-export protein SecB {ECO:0000255|HAMAP-Rule:MF_00821};
GN Name=secB {ECO:0000255|HAMAP-Rule:MF_00821}; OrderedLocusNames=VC_2653;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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}.
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DR EMBL; AE003852; AAF95794.1; -; Genomic_DNA.
DR PIR; C82050; C82050.
DR RefSeq; NP_232281.1; NC_002505.1.
DR RefSeq; WP_000796512.1; NZ_LT906614.1.
DR AlphaFoldDB; Q9KNS8; -.
DR SMR; Q9KNS8; -.
DR STRING; 243277.VC_2653; -.
DR DNASU; 2615670; -.
DR EnsemblBacteria; AAF95794; AAF95794; VC_2653.
DR GeneID; 57741250; -.
DR KEGG; vch:VC_2653; -.
DR PATRIC; fig|243277.26.peg.2529; -.
DR eggNOG; COG1952; Bacteria.
DR HOGENOM; CLU_111574_1_0_6; -.
DR OMA; CPNVLFP; -.
DR BioCyc; VCHO:VC2653-MON; -.
DR Proteomes; UP000000584; Chromosome 1.
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; Reference proteome; Translocation;
KW Transport.
FT CHAIN 1..154
FT /note="Protein-export protein SecB"
FT /id="PRO_0000055420"
SQ SEQUENCE 154 AA; 17035 MW; A7B6B2CCF0DB8B38 CRC64;
MAEAAQAPQQ QFAIQRIYLK DVSFEAPSSP VMFQKEWNPD VKLDLDTQSR ELGQGVYEVV
LRLTVTVKNA EETAFLCEVQ QAGIFSAEQM EAGQLAHCLG AFCPNILFPY ARETISSLVV
KGTFPQLNLA PVNFDALFMN YLQQQAQEGA TANA