ID   SECB1_GLUOX             Reviewed;         173 AA.
AC   Q5FPS3;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Protein-export protein SecB 1 {ECO:0000255|HAMAP-Rule:MF_00821};
GN   Name=secB1 {ECO:0000255|HAMAP-Rule:MF_00821}; OrderedLocusNames=GOX1885;
OS   Gluconobacter oxydans (strain 621H) (Gluconobacter suboxydans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=290633;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=621H;
RX   PubMed=15665824; DOI=10.1038/nbt1062;
RA   Prust C., Hoffmeister M., Liesegang H., Wiezer A., Fricke W.F.,
RA   Ehrenreich A., Gottschalk G., Deppenmeier U.;
RT   "Complete genome sequence of the acetic acid bacterium Gluconobacter
RT   oxydans.";
RL   Nat. Biotechnol. 23:195-200(2005).
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; CP000009; AAW61623.1; -; Genomic_DNA.
DR   RefSeq; WP_011253404.1; NZ_LT900338.1.
DR   AlphaFoldDB; Q5FPS3; -.
DR   SMR; Q5FPS3; -.
DR   STRING; 290633.GOX1885; -.
DR   EnsemblBacteria; AAW61623; AAW61623; GOX1885.
DR   KEGG; gox:GOX1885; -.
DR   eggNOG; COG1952; Bacteria.
DR   HOGENOM; CLU_111574_0_0_5; -.
DR   OMA; NIDVQAN; -.
DR   Proteomes; UP000006375; 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; Reference proteome; Translocation;
KW   Transport.
FT   CHAIN           1..173
FT                   /note="Protein-export protein SecB 1"
FT                   /id="PRO_0000055375"
SQ   SEQUENCE   173 AA;  18667 MW;  6B48E8A743A1CFEC CRC64;
     MSENTTDNAA LGQENVPAMP LAINLQYTKD LSFEVPAGAS IFATLRSAPQ ISVNIDVQAN
     RLEEDQAVYE VALAVRAEAA EPPAQEGGQA GRTVFIAELT YAAVVTLNNP PQELIEPILL
     VEVPRLIFPY VRSIVSDVTR DGGFPPVVLQ PIDFVALWQA KRAQQFPEPA GEA