ID A0A1R1QDT8_9BACI Unreviewed; 211 AA.
AC A0A1R1QDT8; A0A1R1S0J7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Adapter protein MecA {ECO:0000256|HAMAP-Rule:MF_01124};
GN Name=mecA {ECO:0000256|HAMAP-Rule:MF_01124};
GN ORFNames=BTA30_05595 {ECO:0000313|EMBL:OMI31769.1}, BW143_17090
GN {ECO:0000313|EMBL:OMI01409.1};
OS Bacillus swezeyi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1925020 {ECO:0000313|EMBL:OMI01409.1, ECO:0000313|Proteomes:UP000187367};
RN [1] {ECO:0000313|EMBL:OMI01409.1, ECO:0000313|Proteomes:UP000187367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-41282 {ECO:0000313|EMBL:OMI01409.1,
RC ECO:0000313|Proteomes:UP000187367}, and NRRL B-41294
RC {ECO:0000313|EMBL:OMI31769.1, ECO:0000313|Proteomes:UP000187536};
RA Dunlap C.;
RT "Bacillus phylogenomics.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:OMI01409.1}.
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DR EMBL; MTJL01000036; OMI01409.1; -; Genomic_DNA.
DR EMBL; MRBK01000005; OMI31769.1; -; Genomic_DNA.
DR RefSeq; WP_076760283.1; NZ_MTJL01000036.1.
DR AlphaFoldDB; A0A1R1QDT8; -.
DR OrthoDB; 2360201at2; -.
DR Proteomes; UP000187367; Unassembled WGS sequence.
DR Proteomes; UP000187536; 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|ARBA:ARBA00023287, ECO:0000256|HAMAP-
KW Rule:MF_01124}; Sporulation {ECO:0000256|HAMAP-Rule:MF_01124}.
SQ SEQUENCE 211 AA; 24921 MW; B140503EB2C9C088 CRC64;
MEIERINEHT VKFYISYGDI EDRGFDREEI WYNRERSEEL FWEMMDEVHE EEEFAVEGPL
WIQVQALDKG LEIIVTRAQL SKDGQKLELP IPEDKKQDAA EESLDALLED FQKEEAEEQK
LQFVLKFADF EDLISLSKMT ISGCQTTLYS HENRYYLFVD FNELPDEEVE NQLSILLEYA
SESKMTIHML KEYGKLVAAD HALHTIKKHF A
//
