ID   SECB_SACD2              Reviewed;         168 AA.
AC   Q21NG8;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Protein-export protein SecB {ECO:0000255|HAMAP-Rule:MF_00821};
GN   Name=secB {ECO:0000255|HAMAP-Rule:MF_00821}; OrderedLocusNames=Sde_0497;
OS   Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC   Cellvibrionaceae; Saccharophagus.
OX   NCBI_TaxID=203122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-40 / ATCC 43961 / DSM 17024;
RX   PubMed=18516288; DOI=10.1371/journal.pgen.1000087;
RA   Weiner R.M., Taylor L.E. II, Henrissat B., Hauser L., Land M.,
RA   Coutinho P.M., Rancurel C., Saunders E.H., Longmire A.G., Zhang H.,
RA   Bayer E.A., Gilbert H.J., Larimer F., Zhulin I.B., Ekborg N.A., Lamed R.,
RA   Richardson P.M., Borovok I., Hutcheson S.;
RT   "Complete genome sequence of the complex carbohydrate-degrading marine
RT   bacterium, Saccharophagus degradans strain 2-40 T.";
RL   PLoS Genet. 4:E1000087-E1000087(2008).
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; CP000282; ABD79761.1; -; Genomic_DNA.
DR   RefSeq; WP_011466982.1; NC_007912.1.
DR   AlphaFoldDB; Q21NG8; -.
DR   SMR; Q21NG8; -.
DR   STRING; 203122.Sde_0497; -.
DR   EnsemblBacteria; ABD79761; ABD79761; Sde_0497.
DR   KEGG; sde:Sde_0497; -.
DR   eggNOG; COG1952; Bacteria.
DR   HOGENOM; CLU_111574_1_0_6; -.
DR   OMA; CPNVLFP; -.
DR   OrthoDB; 1624074at2; -.
DR   Proteomes; UP000001947; 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..168
FT                   /note="Protein-export protein SecB"
FT                   /id="PRO_1000062514"
SQ   SEQUENCE   168 AA;  17887 MW;  E1ECC750AF73A1EE CRC64;
     MSEENTTNNE AAAAEGKAPA GFGIKRVFTK DLSFEVPAGL GAFSLQGQPN VGQDLNTQIN
     RVDDTHYEVV LKVTVTVKMG EDKVAFLAEV HQAGIFQVVG IEGPQLQQVL STACPQILFP
     YVRETIDSLA VRGGFAPVLL PQINFDALFV QAVAQAKAQA DSQAEADA