ID K6CCG3_9BACI Unreviewed; 224 AA.
AC K6CCG3;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=Adapter protein MecA {ECO:0000256|HAMAP-Rule:MF_01124};
GN Name=mecA {ECO:0000256|HAMAP-Rule:MF_01124};
GN ORFNames=BABA_12311 {ECO:0000313|EMBL:EKN68835.1};
OS Neobacillus bataviensis LMG 21833.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Neobacillus.
OX NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN68835.1, ECO:0000313|Proteomes:UP000006316};
RN [1] {ECO:0000313|EMBL:EKN68835.1, ECO:0000313|Proteomes:UP000006316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX PubMed=23087684;
RA Heylen K., Keltjens J.;
RT "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT reduction in Bacillus.";
RL Front. Microbiol. 3:371-371(2012).
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:0000256|HAMAP-Rule:MF_01124}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC 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. {ECO:0000256|HAMAP-Rule:MF_01124}.
CC -!- SIMILARITY: Belongs to the MecA family. {ECO:0000256|ARBA:ARBA00005397,
CC ECO:0000256|HAMAP-Rule:MF_01124}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKN68835.1}.
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DR EMBL; AJLS01000063; EKN68835.1; -; Genomic_DNA.
DR RefSeq; WP_007085476.1; NZ_AJLS01000063.1.
DR AlphaFoldDB; K6CCG3; -.
DR STRING; 1117379.BABA_12311; -.
DR PATRIC; fig|1117379.3.peg.2566; -.
DR eggNOG; COG4862; Bacteria.
DR OrthoDB; 2360201at2; -.
DR Proteomes; UP000006316; Unassembled WGS sequence.
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; ADAPTER PROTEIN MECA; 1.
DR PANTHER; PTHR39161:SF1; ADAPTER PROTEIN MECA; 1.
DR Pfam; PF05389; MecA; 1.
DR PIRSF; PIRSF029008; MecA; 1.
PE 3: Inferred from homology;
KW Competence {ECO:0000256|HAMAP-Rule:MF_01124};
KW Reference proteome {ECO:0000313|Proteomes:UP000006316};
KW Sporulation {ECO:0000256|HAMAP-Rule:MF_01124}.
SQ SEQUENCE 224 AA; 26680 MW; 7AB001C0DE9BF7F0 CRC64;
MEIERINENT VKFYISYGDI EERGFDREEI WYNRERSEEL FWEMMDEVHG EEDFVAEGPL
WIQVQALDKG LEVLVTKAQL SKDGQKFELP IPTDKLKDIP VDGKIEELLD QHFNPDHPDD
DDDLLLEEET LEFLLAFKDF EDVISLSNRA GLDDLVTKLY HFEGRYYLYI EFPEDLFEED
EIDDLLSVLL EYGYETQLTI HRVHEYGKEI ISNDVFDELR KYFS
//
