ID   SECB_PSEFS              Reviewed;         159 AA.
AC   C3K7C1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Protein-export protein SecB {ECO:0000255|HAMAP-Rule:MF_00821};
GN   Name=secB {ECO:0000255|HAMAP-Rule:MF_00821}; OrderedLocusNames=PFLU_0340;
OS   Pseudomonas fluorescens (strain SBW25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=216595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SBW25;
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.-X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A.C., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(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}.
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DR   EMBL; AM181176; CAY46617.1; -; Genomic_DNA.
DR   RefSeq; WP_012721755.1; NC_012660.1.
DR   AlphaFoldDB; C3K7C1; -.
DR   SMR; C3K7C1; -.
DR   STRING; 216595.PFLU_0340; -.
DR   PRIDE; C3K7C1; -.
DR   EnsemblBacteria; CAY46617; CAY46617; PFLU_0340.
DR   KEGG; pfs:PFLU_0340; -.
DR   eggNOG; COG1952; Bacteria.
DR   HOGENOM; CLU_111574_1_0_6; -.
DR   OMA; CPNVLFP; -.
DR   OrthoDB; 1624074at2; -.
DR   Proteomes; UP000002332; 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..159
FT                   /note="Protein-export protein SecB"
FT                   /id="PRO_1000213108"
SQ   SEQUENCE   159 AA;  17626 MW;  3B8013A264B9BC76 CRC64;
     MTDQQNTEAA EAQGPQFSLQ RIYVRDLSFE APKSPAIFRQ EWTPSVALDL NTRQKALEGD
     FHEVVLTLSV TVKNGEEVAF IAEVQQAGIF LIQGLDEASM SHTLGAFCPN ILFPYARETL
     DSLVTRGSFP ALMLAPVNFD ALYAQELQRM QQEGSSTVQ