ID   SECB2_FRATN             Reviewed;         147 AA.
AC   A0Q810;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Protein-export protein SecB 2 {ECO:0000255|HAMAP-Rule:MF_00821};
GN   Name=secB2 {ECO:0000255|HAMAP-Rule:MF_00821}; OrderedLocusNames=FTN_1510;
OS   Francisella tularensis subsp. novicida (strain U112).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=401614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=U112;
RX   PubMed=17550600; DOI=10.1186/gb-2007-8-6-r102;
RA   Rohmer L., Fong C., Abmayr S., Wasnick M., Larson Freeman T.J., Radey M.,
RA   Guina T., Svensson K., Hayden H.S., Jacobs M., Gallagher L.A., Manoil C.,
RA   Ernst R.K., Drees B., Buckley D., Haugen E., Bovee D., Zhou Y., Chang J.,
RA   Levy R., Lim R., Gillett W., Guenthener D., Kang A., Shaffer S.A.,
RA   Taylor G., Chen J., Gallis B., D'Argenio D.A., Forsman M., Olson M.V.,
RA   Goodlett D.R., Kaul R., Miller S.I., Brittnacher M.J.;
RT   "Comparison of Francisella tularensis genomes reveals evolutionary events
RT   associated with the emergence of human pathogenic strains.";
RL   Genome Biol. 8:R102.1-R102.16(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}.
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DR   EMBL; CP000439; ABK90375.1; -; Genomic_DNA.
DR   RefSeq; WP_003040510.1; NZ_CP009633.1.
DR   AlphaFoldDB; A0Q810; -.
DR   SMR; A0Q810; -.
DR   EnsemblBacteria; ABK90375; ABK90375; FTN_1510.
DR   KEGG; ftn:FTN_1510; -.
DR   OMA; NIDVQAN; -.
DR   OrthoDB; 1624074at2; -.
DR   BioCyc; FTUL401614:G1G75-1558-MON; -.
DR   Proteomes; UP000000762; 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; Translocation; Transport.
FT   CHAIN           1..147
FT                   /note="Protein-export protein SecB 2"
FT                   /id="PRO_0000318232"
SQ   SEQUENCE   147 AA;  16696 MW;  738CE7446D0695FF CRC64;
     MQNNEIQPSF LIQKVYTKDV SFETINSPAC FKEQWNPSSD FNIDINTTKI NNENFELDLT
     ITVTTKNNET NVYIAEVTQS GIFTITGMSE EQIDSVLNTY CANTLFPYAK RIIDSSIIKG
     GFLPLNLAPI NFDAIYLQKK SSPKREH