SECB_HAHCH
ID SECB_HAHCH Reviewed; 159 AA.
AC Q2SMA3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Protein-export protein SecB {ECO:0000255|HAMAP-Rule:MF_00821};
GN Name=secB {ECO:0000255|HAMAP-Rule:MF_00821}; OrderedLocusNames=HCH_01356;
OS Hahella chejuensis (strain KCTC 2396).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Hahellaceae; Hahella.
OX NCBI_TaxID=349521;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2396;
RX PubMed=16352867; DOI=10.1093/nar/gki1016;
RA Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA Oh T.K., Kim J.F.;
RT "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT algicidal agent.";
RL Nucleic Acids Res. 33:7066-7073(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 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; CP000155; ABC28221.1; -; Genomic_DNA.
DR RefSeq; WP_011395294.1; NC_007645.1.
DR AlphaFoldDB; Q2SMA3; -.
DR SMR; Q2SMA3; -.
DR STRING; 349521.HCH_01356; -.
DR PRIDE; Q2SMA3; -.
DR EnsemblBacteria; ABC28221; ABC28221; HCH_01356.
DR KEGG; hch:HCH_01356; -.
DR eggNOG; COG1952; Bacteria.
DR HOGENOM; CLU_111574_1_0_6; -.
DR OMA; CPNVLFP; -.
DR OrthoDB; 1624074at2; -.
DR Proteomes; UP000000238; 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..159
FT /note="Protein-export protein SecB"
FT /id="PRO_0000318239"
SQ SEQUENCE 159 AA; 17671 MW; 23A7D9AB3D40971A CRC64;
MSENAEAPKQ PVFALQRIYL KDLSFESPNS PAVFQSEWKP QVNMDLNTEN KKVSDNQWEV
VLTLTITAKL ADKTAFVIEV QQAGVFMIDG LSPQQLAQTL GAFCPNILFP YARETIDMLA
VKGSFPALML QPVNFDAIYA EAVKRQQAQQ AAPAEEAKH