ID   SECB_BORA1              Reviewed;         172 AA.
AC   Q2L0A9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Protein-export protein SecB {ECO:0000255|HAMAP-Rule:MF_00821};
GN   Name=secB {ECO:0000255|HAMAP-Rule:MF_00821}; OrderedLocusNames=BAV0240;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=197N;
RX   PubMed=16885469; DOI=10.1128/jb.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA   Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA   Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA   Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT   with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT   extensive diversity in surface structures associated with host
RT   interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ47845.1; -; Genomic_DNA.
DR   RefSeq; WP_012415943.1; NC_010645.1.
DR   AlphaFoldDB; Q2L0A9; -.
DR   SMR; Q2L0A9; -.
DR   STRING; 360910.BAV0240; -.
DR   EnsemblBacteria; CAJ47845; CAJ47845; BAV0240.
DR   GeneID; 41392169; -.
DR   KEGG; bav:BAV0240; -.
DR   eggNOG; COG1952; Bacteria.
DR   HOGENOM; CLU_111574_1_0_4; -.
DR   OMA; CPNVLFP; -.
DR   OrthoDB; 1624074at2; -.
DR   Proteomes; UP000001977; 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..172
FT                   /note="Protein-export protein SecB"
FT                   /id="PRO_1000062453"
SQ   SEQUENCE   172 AA;  18914 MW;  23022A943AC2AD55 CRC64;
     MADQDQNTQQ TGSEAPAFNL QRVYLKDLSV EMPNAPHIFL EQEGPAVEVT INVGGQRLAE
     TVFESTVTVT VTTRVNDKVL YLVEGTQAGI FELANIPPEQ MDPILGIVCP TMLYPYLRAN
     VADAITRTSL PALHLTEVNF QALYEQRLAE MAQQQEQSAD SGIILPPSAT RQ