SECB_PARPJ
ID SECB_PARPJ Reviewed; 156 AA.
AC B2SX18;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
DE RecName: Full=Protein-export protein SecB {ECO:0000255|HAMAP-Rule:MF_00821};
GN Name=secB {ECO:0000255|HAMAP-Rule:MF_00821}; OrderedLocusNames=Bphyt_0537;
OS Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS (Burkholderia phytofirmans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=398527;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17436 / LMG 22146 / PsJN;
RX PubMed=21551308; DOI=10.1128/jb.05055-11;
RA Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.;
RT "Complete genome sequence of the plant growth-promoting endophyte
RT Burkholderia phytofirmans strain PsJN.";
RL J. Bacteriol. 193:3383-3384(2011).
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; CP001052; ACD14962.1; -; Genomic_DNA.
DR RefSeq; WP_007179465.1; NC_010681.1.
DR AlphaFoldDB; B2SX18; -.
DR SMR; B2SX18; -.
DR STRING; 398527.Bphyt_0537; -.
DR EnsemblBacteria; ACD14962; ACD14962; Bphyt_0537.
DR KEGG; bpy:Bphyt_0537; -.
DR eggNOG; COG1952; Bacteria.
DR HOGENOM; CLU_111574_1_0_4; -.
DR OMA; NIDVQAN; -.
DR OrthoDB; 1624074at2; -.
DR Proteomes; UP000001739; Chromosome 1.
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..156
FT /note="Protein-export protein SecB"
FT /id="PRO_1000134370"
SQ SEQUENCE 156 AA; 17218 MW; B2DC8FCFC95FD382 CRC64;
MSDENNQPFF NIQRIYLKDM SLEQPNSPGI FLEQEMPSVE VEVDVKAERL ADTVFEILVT
GTVTAKVSDK VAFLIEAKQA GIFDIRNIPA EQIDPLVGIA CPTILFPYLR SNIADAITRA
GFPPIHLAEI NFQALYEQRL AQMGGQDGAA QNGVTH