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MECA_ALKPO
ID   MECA_ALKPO              Reviewed;         217 AA.
AC   O66042; D3FV22;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Adapter protein MecA {ECO:0000255|HAMAP-Rule:MF_01124};
GN   Name=mecA {ECO:0000255|HAMAP-Rule:MF_01124}; OrderedLocusNames=BpOF4_01905;
OS   Alkalihalophilus pseudofirmus (strain ATCC BAA-2126 / JCM 17055 / OF4)
OS   (Bacillus pseudofirmus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalophilus.
OX   NCBI_TaxID=398511;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9443601; DOI=10.1016/s0005-2760(97)00086-6;
RA   Guo D., Tropp B.E.;
RT   "Cloning of the Bacillus firmus OF4 cls gene and characterization of its
RT   gene product.";
RL   Biochim. Biophys. Acta 1389:34-42(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2126 / JCM 17055 / OF4;
RX   PubMed=21951522; DOI=10.1111/j.1462-2920.2011.02591.x;
RA   Janto B., Ahmed A., Ito M., Liu J., Hicks D.B., Pagni S., Fackelmayer O.J.,
RA   Smith T.A., Earl J., Elbourne L.D., Hassan K., Paulsen I.T., Kolsto A.B.,
RA   Tourasse N.J., Ehrlich G.D., Boissy R., Ivey D.M., Li G., Xue Y., Ma Y.,
RA   Hu F.Z., Krulwich T.A.;
RT   "Genome of alkaliphilic Bacillus pseudofirmus OF4 reveals adaptations that
RT   support the ability to grow in an external pH range from 7.5 to 11.4.";
RL   Environ. Microbiol. 13:3289-3309(2011).
CC   -!- FUNCTION: Enables the recognition and targeting of unfolded and
CC       aggregated proteins to the ClpC protease or to other proteins involved
CC       in proteolysis. Acts negatively in the development of competence by
CC       binding ComK and recruiting it to the ClpCP protease. When
CC       overexpressed, inhibits sporulation. Also involved in Spx degradation
CC       by ClpC. {ECO:0000255|HAMAP-Rule:MF_01124}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01124}.
CC   -!- DOMAIN: The N-terminal domain has binding sites for ComK and probably
CC       for unfolded/aggregated proteins; the C-terminal domain interacts with
CC       ClpC.
CC   -!- SIMILARITY: Belongs to the MecA family. {ECO:0000255|HAMAP-
CC       Rule:MF_01124}.
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DR   EMBL; U88888; AAC05443.1; -; Genomic_DNA.
DR   EMBL; CP001878; ADC48448.1; -; Genomic_DNA.
DR   RefSeq; WP_012959726.1; NC_013791.2.
DR   AlphaFoldDB; O66042; -.
DR   SMR; O66042; -.
DR   STRING; 398511.BpOF4_01905; -.
DR   EnsemblBacteria; ADC48448; ADC48448; BpOF4_01905.
DR   KEGG; bpf:BpOF4_01905; -.
DR   eggNOG; COG4862; Bacteria.
DR   HOGENOM; CLU_071496_2_1_9; -.
DR   OMA; EFFYTVM; -.
DR   OrthoDB; 1678325at2; -.
DR   Proteomes; UP000001544; Chromosome.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR   GO; GO:0045808; P:negative regulation of establishment of competence for transformation; IEA:UniProtKB-UniRule.
DR   GO; GO:0042174; P:negative regulation of sporulation resulting in formation of a cellular spore; IEA:UniProtKB-UniRule.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.1950; -; 1.
DR   HAMAP; MF_01124; MecA; 1.
DR   InterPro; IPR038471; MecA_C_sf.
DR   InterPro; IPR008681; Neg-reg_MecA.
DR   PANTHER; PTHR39161; PTHR39161; 1.
DR   Pfam; PF05389; MecA; 1.
DR   PIRSF; PIRSF029008; MecA; 1.
PE   3: Inferred from homology;
KW   Competence; Reference proteome; Sporulation.
FT   CHAIN           1..217
FT                   /note="Adapter protein MecA"
FT                   /id="PRO_0000212266"
SQ   SEQUENCE   217 AA;  25758 MW;  CA26A703A2C37949 CRC64;
     MDIERVNDTT IKFFITYKDI EDRGFDRDEI WYNRERGEEL FFEMMNEAND RDEFELDGPL
     WIQVHALDKG LEIVVTRGQV SDGNVKLEIP VSQDKENTDE NIVDLMTGHS SEDDEGIDTD
     QLEIVIGFND FEDIISLSHN FFIDDLENEL YHFEGRYYLH VLFNDDQYNE DEQDDMLSQM
     LEYGYETDLS IHRMQEYGKE IIGEYALKHL RGHFPQN
 
 
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