SECB_PSEAB
ID SECB_PSEAB Reviewed; 163 AA.
AC Q02EN8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Protein-export protein SecB {ECO:0000255|HAMAP-Rule:MF_00821};
GN Name=secB {ECO:0000255|HAMAP-Rule:MF_00821}; OrderedLocusNames=PA14_67720;
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(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; CP000438; ABJ14511.1; -; Genomic_DNA.
DR RefSeq; WP_003096050.1; NZ_CP034244.1.
DR AlphaFoldDB; Q02EN8; -.
DR SMR; Q02EN8; -.
DR PRIDE; Q02EN8; -.
DR EnsemblBacteria; ABJ14511; ABJ14511; PA14_67720.
DR KEGG; pau:PA14_67720; -.
DR HOGENOM; CLU_111574_1_0_6; -.
DR OMA; CPNVLFP; -.
DR BioCyc; PAER208963:G1G74-5711-MON; -.
DR Proteomes; UP000000653; 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..163
FT /note="Protein-export protein SecB"
FT /id="PRO_1000062492"
SQ SEQUENCE 163 AA; 18146 MW; 577A86F6C2EB2384 CRC64;
MTEQATNGAA DEQQPQFSLQ RIYLRDLSFE SPKSPEIFRQ EWNPSISLDL NTRQKQLDGD
FYEVVLTVSV TVKNGEDTTA FIAEVQQAGI FLIKNLDPSS MSHTLGAFCP NILFPYAREA
LDNLVVRGSF PALMLSPVNF DALYAQEIAR MQASGEIPTP SVQ