ID   MECA_OCEIH              Reviewed;         192 AA.
AC   Q8EQ97;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Adapter protein MecA {ECO:0000255|HAMAP-Rule:MF_01124};
GN   Name=mecA {ECO:0000255|HAMAP-Rule:MF_01124}; OrderedLocusNames=OB1811;
OS   Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC
OS   3954 / HTE831).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX   NCBI_TaxID=221109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831;
RX   PubMed=12235376; DOI=10.1093/nar/gkf526;
RA   Takami H., Takaki Y., Uchiyama I.;
RT   "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya Ridge
RT   and its unexpected adaptive capabilities to extreme environments.";
RL   Nucleic Acids Res. 30:3927-3935(2002).
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; BA000028; BAC13767.1; -; Genomic_DNA.
DR   RefSeq; WP_011066209.1; NC_004193.1.
DR   AlphaFoldDB; Q8EQ97; -.
DR   SMR; Q8EQ97; -.
DR   STRING; 221109.22777495; -.
DR   EnsemblBacteria; BAC13767; BAC13767; BAC13767.
DR   KEGG; oih:OB1811; -.
DR   eggNOG; COG4862; Bacteria.
DR   HOGENOM; CLU_071496_3_0_9; -.
DR   OMA; IEMQVKL; -.
DR   OrthoDB; 1678325at2; -.
DR   PhylomeDB; Q8EQ97; -.
DR   Proteomes; UP000000822; 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   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; 2.
DR   PIRSF; PIRSF029008; MecA; 1.
PE   3: Inferred from homology;
KW   Competence; Reference proteome.
FT   CHAIN           1..192
FT                   /note="Adapter protein MecA"
FT                   /id="PRO_0000212275"
SQ   SEQUENCE   192 AA;  22906 MW;  DD3608F6F68759C1 CRC64;
     MRIERVSTDQ FKIFLTFDDL IERGFTREDL WHDASNVRSL FSDMMYEASS ELGIELEGML
     LVQVHLMQAQ GMHIFVTQQY EDNSEDEDYI EMKVTLDESK ELIFSFMDFE DIISVTSYLD
     PMGLENIRLY YMEDRYYMIL DHIELSRVDK EDIIGVMSEY ANPSIVTSHR IEEYGKLIME
     ENTVQQIKRF FY