MECA1_BACCR
ID MECA1_BACCR Reviewed; 227 AA.
AC Q81GK5;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Adapter protein MecA 1;
GN Name=mecA1; OrderedLocusNames=BC_1190;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(2003).
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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
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:0000305}.
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DR EMBL; AE016877; AAP08176.1; -; Genomic_DNA.
DR RefSeq; NP_830975.1; NC_004722.1.
DR RefSeq; WP_000350713.1; NZ_CP034551.1.
DR AlphaFoldDB; Q81GK5; -.
DR SMR; Q81GK5; -.
DR STRING; 226900.BC_1190; -.
DR EnsemblBacteria; AAP08176; AAP08176; BC_1190.
DR GeneID; 67505908; -.
DR KEGG; bce:BC1190; -.
DR PATRIC; fig|226900.8.peg.1157; -.
DR HOGENOM; CLU_071496_2_1_9; -.
DR OMA; EFFYTVM; -.
DR Proteomes; UP000001417; 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..227
FT /note="Adapter protein MecA 1"
FT /id="PRO_0000212262"
SQ SEQUENCE 227 AA; 27010 MW; 00C951497F3C0615 CRC64;
MDIERINDHT MKFFITYIDI EDRGFNREEI WYDRERSEEL FWEMMDEARD HDDFFIDGPL
WIQVQAVDKG IEVLVTKAEL SKDGQKLELP IGVDKIIDIP LDEGIESLFQ QELVEEVEEQ
TGTNFNEDGT FGFLIKFNDF EDVISLSHRL IFEDIKDELY SFEDRYYVYV EFDEVLHDEE
EIDRILSIIL EYGEESTLTI HRVSEYGKQI VKEHALETIR NNFPAKT