ID   SECB2_FRATT             Reviewed;         149 AA.
AC   Q5NE99;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Protein-export protein SecB 2 {ECO:0000255|HAMAP-Rule:MF_00821};
GN   Name=secB2 {ECO:0000255|HAMAP-Rule:MF_00821}; OrderedLocusNames=FTT_1749;
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4;
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA   Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA   Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA   Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA   Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(2005).
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; AJ749949; CAG46382.1; -; Genomic_DNA.
DR   RefSeq; WP_003013731.1; NZ_CP010290.1.
DR   RefSeq; YP_170643.1; NC_006570.2.
DR   AlphaFoldDB; Q5NE99; -.
DR   SMR; Q5NE99; -.
DR   IntAct; Q5NE99; 3.
DR   STRING; 177416.FTT_1749; -.
DR   DNASU; 3191208; -.
DR   EnsemblBacteria; CAG46382; CAG46382; FTT_1749.
DR   GeneID; 60806227; -.
DR   KEGG; ftu:FTT_1749; -.
DR   eggNOG; COG1952; Bacteria.
DR   OMA; CPNVLFP; -.
DR   Proteomes; UP000001174; 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..149
FT                   /note="Protein-export protein SecB 2"
FT                   /id="PRO_0000055374"
SQ   SEQUENCE   149 AA;  16900 MW;  C693FECCA06D0CBC CRC64;
     MDQQAQPQFQ IQKVYVKDLS FSIPNSDKIW TTNWKPELHT DLKVEATKLP EENTYETVLT
     LEVKVENDGM VAFEAEVKQA GIFTVANMQE AQIEHAKKAF CPNILYHYAR EAISDLVISG
     GFPQLCLSAV NFDAMYQDSL KESADSKQH