ID   SECB2_POLNA             Reviewed;         162 AA.
AC   A1VKS9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 2.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Protein-export protein SecB 2 {ECO:0000255|HAMAP-Rule:MF_00821};
GN   Name=secB2 {ECO:0000255|HAMAP-Rule:MF_00821}; OrderedLocusNames=Pnap_0940;
OS   Polaromonas naphthalenivorans (strain CJ2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2;
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(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   -!- SEQUENCE CAUTION:
CC       Sequence=ABM36257.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000529; ABM36257.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_041376525.1; NC_008781.1.
DR   AlphaFoldDB; A1VKS9; -.
DR   SMR; A1VKS9; -.
DR   STRING; 365044.Pnap_0940; -.
DR   EnsemblBacteria; ABM36257; ABM36257; Pnap_0940.
DR   KEGG; pna:Pnap_0940; -.
DR   eggNOG; COG1952; Bacteria.
DR   HOGENOM; CLU_111574_1_0_4; -.
DR   OrthoDB; 1624074at2; -.
DR   Proteomes; UP000000644; 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..162
FT                   /note="Protein-export protein SecB 2"
FT                   /id="PRO_0000318255"
SQ   SEQUENCE   162 AA;  17924 MW;  8D0D899F6B703B7D CRC64;
     MPDENKQPLF QIQRVYLKGL SLEQPNSPAI FLEEQSPTLE VAVSTIAEQQ ADGIFESTVT
     VSVTAKIRDK VAFLVEAKQS GIFEIRHLPA EQLNPALGIG CPTILYPYLR ANIADAITRA
     GFPPVHLSEI NFQAFYLQQQ KNKMATQPGQ TAEEPAMALE QE