ID   SECB_BRADU              Reviewed;         161 AA.
AC   Q89WN7;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Protein-export protein SecB {ECO:0000255|HAMAP-Rule:MF_00821};
GN   Name=secB {ECO:0000255|HAMAP-Rule:MF_00821}; OrderedLocusNames=bll0641;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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; BA000040; BAC45906.1; -; Genomic_DNA.
DR   RefSeq; NP_767281.1; NC_004463.1.
DR   RefSeq; WP_011083468.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89WN7; -.
DR   SMR; Q89WN7; -.
DR   STRING; 224911.27348890; -.
DR   EnsemblBacteria; BAC45906; BAC45906; BAC45906.
DR   GeneID; 64020503; -.
DR   KEGG; bja:bll0641; -.
DR   PATRIC; fig|224911.44.peg.10; -.
DR   eggNOG; COG1952; Bacteria.
DR   HOGENOM; CLU_111574_0_0_5; -.
DR   InParanoid; Q89WN7; -.
DR   OMA; CPNVLFP; -.
DR   PhylomeDB; Q89WN7; -.
DR   Proteomes; UP000002526; 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..161
FT                   /note="Protein-export protein SecB"
FT                   /id="PRO_0000055351"
SQ   SEQUENCE   161 AA;  17456 MW;  F9B4BE8C3D372416 CRC64;
     MTNGNGTPPE AAPAPQLNVL AQYTKDLSFE NPNAPSSLQQ QGQPPQINIQ INVGANNLSE
     QEFEVTLSVE GKAETAGKVM FSFELAYAGV FRIVNVPKEN LHPLVMIECP RLLFPFAREI
     IATAVRDGGF PPLMLDPVDF VGLYRQNMER QMAAGGQAGQ A