(data stored in ACNUC7421 zone)

SWISSPROT: SECB_PSEHT

ID   SECB_PSEHT              Reviewed;         162 AA.
AC   Q3IIE1;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 73.
DE   RecName: Full=Protein-export protein SecB {ECO:0000255|HAMAP-Rule:MF_00821};
GN   Name=secB {ECO:0000255|HAMAP-Rule:MF_00821};
GN   OrderedLocusNames=PSHAa0369;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(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
CC       that binds to a subset of precursor proteins, maintaining them in
CC       a 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
CC       interacts 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}.
DR   EMBL; CR954246; CAI85467.1; -; Genomic_DNA.
DR   RefSeq; WP_011327080.1; NC_007481.1.
DR   ProteinModelPortal; Q3IIE1; -.
DR   SMR; Q3IIE1; -.
DR   STRING; 326442.PSHAa0369; -.
DR   EnsemblBacteria; CAI85467; CAI85467; PSHAa0369.
DR   GeneID; 32566624; -.
DR   KEGG; pha:PSHAa0369; -.
DR   eggNOG; ENOG4105IX2; Bacteria.
DR   eggNOG; COG1952; LUCA.
DR   HOGENOM; HOG000218192; -.
DR   KO; K03071; -.
DR   OMA; CPNVLFP; -.
DR   OrthoDB; POG091H04FY; -.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051082; F:unfolded protein binding; IEA:InterPro.
DR   GO; GO:0051262; P:protein tetramerization; IEA:InterPro.
DR   GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.420.10; -; 1.
DR   HAMAP; MF_00821; SecB; 1.
DR   InterPro; IPR003708; SecB.
DR   PANTHER; PTHR36918:SF2; PTHR36918:SF2; 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;
DR   PRODOM; Q3IIE1.
DR   SWISS-2DPAGE; Q3IIE1.
KW   Chaperone; Complete proteome; Cytoplasm; Protein transport;
KW   Reference proteome; Translocation; Transport.
FT   CHAIN         1    162       Protein-export protein SecB.
FT                                /FTId=PRO_0000055394.
SQ   SEQUENCE   162 AA;  17940 MW;  5C6CDA6FA6B6F01C CRC64;
     MNEETQNAAA QQETGAQFTI QRIYTKDVSF ETPNSPAIFQ KEWTPEVKLD LDTRSNKLDE
     GVFEVVLALT VTASIGEETA FLCEIQQAGI FTIADVEETQ LAHMLGAFCP NVLFPYAREA
     VSNLVNRGTF PQLNLAPVNF DALFAQYMQQ RTAQAEQASV DA
//

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