MECA_STAAM
ID MECA_STAAM Reviewed; 239 AA.
AC P60184; Q99V92;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Adapter protein MecA {ECO:0000255|HAMAP-Rule:MF_01124};
GN Name=mecA {ECO:0000255|HAMAP-Rule:MF_01124}; OrderedLocusNames=SAV0998;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
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. {ECO:0000255|HAMAP-Rule:MF_01124}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01124}.
CC -!- DOMAIN: The N-terminal domain probably binds unfolded/aggregated
CC proteins; the C-terminal domain interacts with ClpC.
CC -!- SIMILARITY: Belongs to the MecA family. {ECO:0000255|HAMAP-
CC Rule:MF_01124}.
CC -!- CAUTION: This protein is unrelated to the penicillin-binding protein
CC Pbp2a, also called MecA, that confers resistance to methicillin in
CC several strains of S.aureus (MRSA) and is used as a marker for the
CC identification of MRSA isolates. {ECO:0000305}.
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DR EMBL; BA000017; BAB57160.1; -; Genomic_DNA.
DR RefSeq; WP_001217728.1; NC_002758.2.
DR AlphaFoldDB; P60184; -.
DR SMR; P60184; -.
DR World-2DPAGE; 0002:P60184; -.
DR PaxDb; P60184; -.
DR EnsemblBacteria; BAB57160; BAB57160; SAV0998.
DR KEGG; sav:SAV0998; -.
DR HOGENOM; CLU_071496_2_1_9; -.
DR OMA; EFFYTVM; -.
DR PhylomeDB; P60184; -.
DR BioCyc; SAUR158878:SAV_RS05400-MON; -.
DR Proteomes; UP000002481; Chromosome.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; 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; 1.
DR PIRSF; PIRSF029008; MecA; 1.
PE 3: Inferred from homology;
FT CHAIN 1..239
FT /note="Adapter protein MecA"
FT /id="PRO_0000212277"
FT REGION 118..137
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..132
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 239 AA; 28299 MW; 58343EEDDEF5FB44 CRC64;
MRIERVDDTT VKLFITYSDI EARGFSREDL WTNRKRGEEF FWSMMDEINE EEDFVVEGPL
WIQVHAFEKG VEVTISKSKN EDMMNMSDDD ATDQFDEQVQ ELLAQTLEGE DQLEELFEQR
TKEKEAQGSK RQKSSARKNT RTIIVKFNDL EDVINYAYHS NPITTEFEDL LYMVDGTYYY
AVHFDSHVDQ EVINDSYSQL LEFAYPTDRT EVYLNDYAKI IMSHNVTAQV RRYFPETTE