ID   SECB_CERSK              Reviewed;         166 AA.
AC   B9KPW0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Protein-export protein SecB {ECO:0000255|HAMAP-Rule:MF_00821};
GN   Name=secB {ECO:0000255|HAMAP-Rule:MF_00821};
GN   OrderedLocusNames=RSKD131_2635;
OS   Cereibacter sphaeroides (strain KD131 / KCTC 12085) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=557760;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KD131 / KCTC 12085;
RX   PubMed=19028901; DOI=10.1128/jb.01565-08;
RA   Lim S.-K., Kim S.J., Cha S.H., Oh Y.-K., Rhee H.-J., Kim M.-S., Lee J.K.;
RT   "Complete genome sequence of Rhodobacter sphaeroides KD131.";
RL   J. Bacteriol. 191:1118-1119(2009).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001150; ACM02495.1; -; Genomic_DNA.
DR   RefSeq; WP_002721743.1; NC_011963.1.
DR   AlphaFoldDB; B9KPW0; -.
DR   SMR; B9KPW0; -.
DR   EnsemblBacteria; ACM02495; ACM02495; RSKD131_2635.
DR   GeneID; 57471568; -.
DR   GeneID; 67448009; -.
DR   KEGG; rsk:RSKD131_2635; -.
DR   HOGENOM; CLU_111574_0_0_5; -.
DR   OMA; NIDVQAN; -.
DR   Proteomes; UP000001597; 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; Translocation; Transport.
FT   CHAIN           1..166
FT                   /note="Protein-export protein SecB"
FT                   /id="PRO_1000148707"
SQ   SEQUENCE   166 AA;  18659 MW;  7B6AE070B31F2A54 CRC64;
     MTDANGAPAE AAPQIRMQVL AQYVRDMSFE NMVAQKGLQG GDVQPDIQVQ VSLDARKRSV
     EHQYEVITKF KVTSKNKSGS AETLFLLELD YGGIFHVENV PEDQLHPFLL IECPRLLFPF
     VRRIISDVTR DGGFPPLNVD TVDFLALYRM ELARRAEAQK AAQPVQ