ID   SECB1_FRATW             Reviewed;         147 AA.
AC   A4IXL1;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Protein-export protein SecB 1 {ECO:0000255|HAMAP-Rule:MF_00821};
GN   Name=secB1 {ECO:0000255|HAMAP-Rule:MF_00821}; OrderedLocusNames=FTW_0791;
OS   Francisella tularensis subsp. tularensis (strain WY96-3418).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=418136;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WY96-3418;
RX   PubMed=17895988; DOI=10.1371/journal.pone.0000947;
RA   Beckstrom-Sternberg S.M., Auerbach R.K., Godbole S., Pearson J.V.,
RA   Beckstrom-Sternberg J.S., Deng Z., Munk C., Kubota K., Zhou Y., Bruce D.,
RA   Noronha J., Scheuermann R.H., Wang A., Wei X., Wang J., Hao J.,
RA   Wagner D.M., Brettin T.S., Brown N., Gilna P., Keim P.S.;
RT   "Complete genomic characterization of a pathogenic A.II strain of
RT   Francisella tularensis subspecies tularensis.";
RL   PLoS ONE 2:E947-E947(2007).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000608; ABO46663.1; -; Genomic_DNA.
DR   RefSeq; WP_003014455.1; NC_009257.1.
DR   AlphaFoldDB; A4IXL1; -.
DR   SMR; A4IXL1; -.
DR   KEGG; ftw:FTW_0791; -.
DR   HOGENOM; CLU_111574_1_0_6; -.
DR   OMA; NIDVQAN; -.
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; Translocation; Transport.
FT   CHAIN           1..147
FT                   /note="Protein-export protein SecB 1"
FT                   /id="PRO_0000318236"
SQ   SEQUENCE   147 AA;  16699 MW;  59F2E9B60E996778 CRC64;
     MQNNEIQPSF LIQKVYTKDV SFETINSPAC FKEQWNPSSD FNIDINTTKI NDENFELDLT
     ITVTTKNNET NAYIAEVTQS GIFTITSMSE EQIDSVLNTY CANTLFPYAK RIIDSSIIKG
     GFLPLNLAPI NFDAIYLQKK SSPKREH