SECB_VIBC1
ID SECB_VIBC1 Reviewed; 154 AA.
AC A7MX74;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Protein-export protein SecB {ECO:0000255|HAMAP-Rule:MF_00821};
GN Name=secB {ECO:0000255|HAMAP-Rule:MF_00821};
GN OrderedLocusNames=VIBHAR_00123;
OS Vibrio campbellii (strain ATCC BAA-1116).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2902295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA Wilson R.K.;
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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=ABU69171.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000789; ABU69171.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_021017965.1; NC_022269.1.
DR AlphaFoldDB; A7MX74; -.
DR SMR; A7MX74; -.
DR EnsemblBacteria; ABU69171; ABU69171; VIBHAR_00123.
DR KEGG; vha:VIBHAR_00123; -.
DR PATRIC; fig|338187.25.peg.2410; -.
DR OrthoDB; 1624074at2; -.
DR Proteomes; UP000008152; Chromosome I.
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..154
FT /note="Protein-export protein SecB"
FT /id="PRO_0000318270"
SQ SEQUENCE 154 AA; 17191 MW; 5FF586042C9D6381 CRC64;
MAEAAPQDAQ QNFAIQRIFL KDVSFEAPNS PVMFQKEWNP DVKLDLDTQS RELGEGVYEI
VLRLTVTVKN EEETAFLCEV QQGGIFTAEK MEAGQLAHCL GAFCPNILFP YARETISSLV
VKGTFPQLNL APVNFDALFM NYLQQQAQQG EAEA