ID   SECB_RICFE              Reviewed;         152 AA.
AC   Q4UNF2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 1.
DT   04-NOV-2026, entry version 98.
DE   RecName: Full=Protein-export protein SecB {ECO:0000255|HAMAP-Rule:MF_00821};
GN   Name=secB {ECO:0000255|HAMAP-Rule:MF_00821};
GN   OrderedLocusNames=RF_0055;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Rickettsiales; Rickettsiaceae; Rickettsieae; Rickettsia;
OC   spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(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}.
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; CP000053; AAY60906.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4UNF2; -.
DR   SMR; Q4UNF2; -.
DR   STRING; 315456.RF_0055; -.
DR   KEGG; rfe:RF_0055; -.
DR   eggNOG; COG1952; Bacteria.
DR   HOGENOM; CLU_111574_0_0_5; -.
DR   OMA; AADQPMM; -.
DR   OrthoDB; 9795145at2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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   CDD; cd00557; Translocase_SecB; 1.
DR   Gene3D; 3.10.420.10; SecB-like; 1.
DR   HAMAP; MF_00821; SecB; 1.
DR   InterPro; IPR003708; SecB.
DR   InterPro; IPR035958; SecB-like_sf.
DR   NCBIfam; NF004392; secB; 1.
DR   NCBIfam; TIGR00809; secB; 1.
DR   PANTHER; PTHR36918; -; 1.
DR   PANTHER; PTHR36918:SF1; PROTEIN-EXPORT PROTEIN SECB; 1.
DR   Pfam; PF02556; SecB; 1.
DR   PRINTS; PR01594; SECBCHAPRONE.
DR   SUPFAM; SSF54611; SecB-like; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Protein transport; Translocation; Transport.
FT   CHAIN           1..152
FT                   /note="Protein-export protein SecB"
FT                   /id="PRO_0000055409"
SQ   SEQUENCE   152 AA;  17168 MW;  128F224FC74213C1 CRC64;
     MSTINTDTNE AMPHISVNAQ YIKDLSLENP SAPSSLAALE QRPQIDLSLD INITNLSEEN
     FYEVELNIEA TARNEKYKLF QIELKYAGVF NLINIDSEQH PILLSVHCPA MIFPFARKII
     ASCTQDAGFQ PLMIDPIDFG ALYHKKMSEH QN
//