SECB_CELJU
ID SECB_CELJU Reviewed; 167 AA.
AC B3PGW2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Protein-export protein SecB {ECO:0000255|HAMAP-Rule:MF_00821};
GN Name=secB {ECO:0000255|HAMAP-Rule:MF_00821}; OrderedLocusNames=CJA_3557;
OS Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp.
OS cellulosa).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Cellvibrio.
OX NCBI_TaxID=498211;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ueda107;
RX PubMed=18556790; DOI=10.1128/jb.01701-07;
RA DeBoy R.T., Mongodin E.F., Fouts D.E., Tailford L.E., Khouri H.,
RA Emerson J.B., Mohamoud Y., Watkins K., Henrissat B., Gilbert H.J.,
RA Nelson K.E.;
RT "Insights into plant cell wall degradation from the genome sequence of the
RT soil bacterium Cellvibrio japonicus.";
RL J. Bacteriol. 190:5455-5463(2008).
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; CP000934; ACE84835.1; -; Genomic_DNA.
DR RefSeq; WP_012489132.1; NC_010995.1.
DR AlphaFoldDB; B3PGW2; -.
DR SMR; B3PGW2; -.
DR STRING; 498211.CJA_3557; -.
DR EnsemblBacteria; ACE84835; ACE84835; CJA_3557.
DR KEGG; cja:CJA_3557; -.
DR eggNOG; COG1952; Bacteria.
DR HOGENOM; CLU_111574_1_0_6; -.
DR OMA; CPNVLFP; -.
DR OrthoDB; 1624074at2; -.
DR Proteomes; UP000001036; 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..167
FT /note="Protein-export protein SecB"
FT /id="PRO_1000134371"
SQ SEQUENCE 167 AA; 18241 MW; 0C3B00131F42E9D1 CRC64;
MSDENNQQDA QQAAGGPQFA IQRIYLKDLS FETPMGVEAF TKAFKPNIQQ DLNIQANQVE
EGLFEVVLLL TVTARTDNRA VFLVEIKQAG LFAIGGLEGG AVTQLINTAC PQILFPYARE
AIDSILNRGS FPPLMLPPIN FDAVFVQAIS QAQQQAETEK AQGETIN