MECI_STAAN
ID MECI_STAAN Reviewed; 123 AA.
AC P68261; P26598;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Methicillin resistance regulatory protein MecI;
GN Name=mecI; OrderedLocusNames=SA0040;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1544435; DOI=10.1016/0014-5793(92)80039-j;
RA Hiramatsu K., Asada K., Suzuki E., Okonogi K., Yokota T.;
RT "Molecular cloning and nucleotide sequence determination of the regulator
RT region of mecA gene in methicillin-resistant Staphylococcus aureus
RT (MRSA).";
RL FEBS Lett. 298:133-136(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10348769; DOI=10.1128/aac.43.6.1449;
RA Ito T., Katayama Y., Hiramatsu K.;
RT "Cloning and nucleotide sequence determination of the entire mec DNA of
RT pre-methicillin-resistant Staphylococcus aureus N315.";
RL Antimicrob. Agents Chemother. 43:1449-1458(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
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).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), INTERACTION WITH DNA, PROTEIN
RP SEQUENCE OF N-TERMINUS, AND SUBUNIT.
RX PubMed=12881514; DOI=10.1074/jbc.m307199200;
RA Garcia-Castellanos R., Marrero A., Mallorqui-Fernandez G., Potempa J.,
RA Coll M., Gomis-Rueth F.X.;
RT "Three-dimensional structure of MecI. Molecular basis for transcriptional
RT regulation of staphylococcal methicillin resistance.";
RL J. Biol. Chem. 278:39897-39905(2003).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH DNA, AND SUBUNIT.
RX PubMed=14960592; DOI=10.1074/jbc.m313123200;
RA Garcia-Castellanos R., Mallorqui-Fernandez G., Marrero A., Potempa J.,
RA Coll M., Gomis-Rueth F.X.;
RT "On the transcriptional regulation of methicillin resistance: MecI
RT repressor in complex with its operator.";
RL J. Biol. Chem. 279:17888-17896(2004).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) IN COMPLEX WITH DNA.
RX PubMed=16582476; DOI=10.1107/s1744309106009742;
RA Safo M.K., Ko T.-P., Musayev F.N., Zhao Q., Wang A.H.-J., Archer G.L.;
RT "Structure of the MecI repressor from Staphylococcus aureus in complex with
RT the cognate DNA operator of mec.";
RL Acta Crystallogr. F 62:320-324(2006).
CC -!- FUNCTION: Transcriptional repressor that constitutively blocks the
CC transcription of the gene for the penicillin-binding protein MecA.
CC Binds palindromic DNA with the sequence 5'-TACA-[AT]-N-TGTA-3'.
CC Regulates genes involved in antibiotic resistance. Binds DNA as a
CC dimer.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000269|PubMed:12881514,
CC ECO:0000269|PubMed:14960592, ECO:0000269|PubMed:16582476}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- PTM: Upon exposure to beta-lactams, proteolytic cleavage at a single
CC site impairs dimerization and abolishes repressor activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the BlaI transcriptional regulatory family.
CC {ECO:0000305}.
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DR EMBL; X63598; CAA45143.1; -; Genomic_DNA.
DR EMBL; D86934; BAA82218.1; -; Genomic_DNA.
DR EMBL; BA000018; BAB41258.1; -; Genomic_DNA.
DR PIR; S20576; S20576.
DR RefSeq; WP_000369214.1; NC_002745.2.
DR PDB; 1OKR; X-ray; 2.40 A; A/B=1-123.
DR PDB; 1SAX; X-ray; 2.80 A; A/B=1-123.
DR PDB; 1SD6; X-ray; 2.65 A; A/B=1-123.
DR PDB; 1SD7; X-ray; 2.65 A; A/B=1-123.
DR PDB; 2D45; X-ray; 3.80 A; A/B/C/D=1-123.
DR PDBsum; 1OKR; -.
DR PDBsum; 1SAX; -.
DR PDBsum; 1SD6; -.
DR PDBsum; 1SD7; -.
DR PDBsum; 2D45; -.
DR AlphaFoldDB; P68261; -.
DR SMR; P68261; -.
DR EnsemblBacteria; BAB41258; BAB41258; BAB41258.
DR GeneID; 64830977; -.
DR KEGG; sau:SA0040; -.
DR HOGENOM; CLU_119090_2_1_9; -.
DR OMA; GNSREYY; -.
DR EvolutionaryTrace; P68261; -.
DR Proteomes; UP000000751; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005650; BlaI_family.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR34134; PTHR34134; 1.
DR Pfam; PF03965; Penicillinase_R; 1.
DR PIRSF; PIRSF019455; CopR_AtkY; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..123
FT /note="Methicillin resistance regulatory protein MecI"
FT /id="PRO_0000062797"
FT DNA_BIND 7..71
FT /note="H-T-H motif"
FT REGION 74..123
FT /note="Important for dimerization"
FT SITE 101..102
FT /note="Cleavage"
FT /evidence="ECO:0000250"
FT HELIX 10..22
FT /evidence="ECO:0007829|PDB:1OKR"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:1OKR"
FT HELIX 27..37
FT /evidence="ECO:0007829|PDB:1OKR"
FT HELIX 42..54
FT /evidence="ECO:0007829|PDB:1OKR"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:1OKR"
FT STRAND 66..73
FT /evidence="ECO:0007829|PDB:1OKR"
FT HELIX 75..90
FT /evidence="ECO:0007829|PDB:1OKR"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:1OKR"
FT HELIX 110..120
FT /evidence="ECO:0007829|PDB:1OKR"
SQ SEQUENCE 123 AA; 14790 MW; 82FC1C109FD38410 CRC64;
MDNKTYEISS AEWEVMNIIW MKKYASANNI IEEIQMQKDW SPKTIRTLIT RLYKKGFIDR
KKDNKIFQYY SLVEESDIKY KTSKNFINKV YKGGFNSLVL NFVEKEDLSQ DEIEELRNIL
NKK
