SECB_RICTY
ID SECB_RICTY Reviewed; 152 AA.
AC Q68XU4; Q8RLP6;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Protein-export protein SecB {ECO:0000255|HAMAP-Rule:MF_00821};
GN Name=secB {ECO:0000255|HAMAP-Rule:MF_00821}; OrderedLocusNames=RT0062;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA On'gele E.A., Radulovic S., Azad A.F.;
RT "Characterization of the Sec operon of the typhus group Rickettsia.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
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; AY078351; AAL82789.1; -; Genomic_DNA.
DR EMBL; AE017197; AAU03548.1; -; Genomic_DNA.
DR RefSeq; WP_011190535.1; NC_006142.1.
DR AlphaFoldDB; Q68XU4; -.
DR SMR; Q68XU4; -.
DR STRING; 257363.RT0062; -.
DR EnsemblBacteria; AAU03548; AAU03548; RT0062.
DR KEGG; rty:RT0062; -.
DR eggNOG; COG1952; Bacteria.
DR HOGENOM; CLU_111574_0_0_5; -.
DR OMA; CPNVLFP; -.
DR OrthoDB; 1624074at2; -.
DR Proteomes; UP000000604; 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..152
FT /note="Protein-export protein SecB"
FT /id="PRO_0000055411"
FT CONFLICT 6
FT /note="S -> T (in Ref. 1; AAL82789)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 152 AA; 17110 MW; CF6E45E2B145C5C3 CRC64;
MSTINSDTSE AMPHISVNAQ YIKDLSLENP SAPSSLAALD QRPQIDLSLD INITNLSDEN
FYEVELNIEA IARNEKYKLF QIELKYAGVF NLINIDSEQH PILLSVHCPA MIFPFARKII
ASCTQDAGFQ PLMIDPIDFG ALYHKKMSEH QN
