SECB_JANMA
ID SECB_JANMA Reviewed; 164 AA.
AC A6T312;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Protein-export protein SecB {ECO:0000255|HAMAP-Rule:MF_00821};
GN Name=secB {ECO:0000255|HAMAP-Rule:MF_00821}; OrderedLocusNames=mma_3219;
OS Janthinobacterium sp. (strain Marseille) (Minibacterium massiliensis).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Janthinobacterium.
OX NCBI_TaxID=375286;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Marseille;
RX PubMed=17722982; DOI=10.1371/journal.pgen.0030138;
RA Audic S., Robert C., Campagna B., Parinello H., Claverie J.-M., Raoult D.,
RA Drancourt M.;
RT "Genome analysis of Minibacterium massiliensis highlights the convergent
RT evolution of water-living bacteria.";
RL PLoS Genet. 3:1454-1463(2007).
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; CP000269; ABR88669.1; -; Genomic_DNA.
DR RefSeq; WP_012081062.1; NC_009659.1.
DR AlphaFoldDB; A6T312; -.
DR SMR; A6T312; -.
DR STRING; 375286.mma_3219; -.
DR EnsemblBacteria; ABR88669; ABR88669; mma_3219.
DR KEGG; mms:mma_3219; -.
DR eggNOG; COG1952; Bacteria.
DR HOGENOM; CLU_111574_1_0_4; -.
DR OMA; NIDVQAN; -.
DR OrthoDB; 1624074at2; -.
DR BioCyc; JSP375286:MMA_RS16665-MON; -.
DR Proteomes; UP000006388; 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..164
FT /note="Protein-export protein SecB"
FT /id="PRO_1000062481"
SQ SEQUENCE 164 AA; 17991 MW; 0E65B1819D8BF345 CRC64;
MADENLQPLF QIQRVYLKDL SLEQPNSPAI FLEQEQPTIE VAVDVGAQPL AEGIFESTVT
ITVTAKIADK IAFLVEGKQA GIFEIRNIPD EQLDPLLGIG CPNVIYPYLR ANIADAITRA
GFPPVHLSEI NFEVFYQQRL EALAQQQADN SSGIVMADGS AARH