MSRA_STAEP
ID MSRA_STAEP Reviewed; 488 AA.
AC P23212;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Erythromycin resistance ATP-binding protein MsrA;
GN Name=msrA;
OS Staphylococcus epidermidis.
OG Plasmid pUL5050.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1282;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=968;
RX PubMed=2233255; DOI=10.1111/j.1365-2958.1990.tb00696.x;
RA Ross J.I., Eady E.A., Cove J.H., Cunliffe W.J., Baumberg S., Wootton J.C.;
RT "Inducible erythromycin resistance in staphylococci is encoded by a member
RT of the ATP-binding transport super-gene family.";
RL Mol. Microbiol. 4:1207-1214(1990).
CC -!- FUNCTION: Confers resistance to 14-membered ring macrolides (like
CC erythromycin) and to B streptogramins, by acting as an ATP-dependent
CC efflux pump.
CC -!- DOMAIN: Composed of two homologous domains.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; X52085; CAA36304.1; ALT_SEQ; Genomic_DNA.
DR PIR; S11158; YESAEE.
DR RefSeq; WP_063854312.1; NG_047999.1.
DR AlphaFoldDB; P23212; -.
DR SMR; P23212; -.
DR TCDB; 3.A.1.121.1; the atp-binding cassette (abc) superfamily.
DR PRIDE; P23212; -.
DR KEGG; ag:CAA36304; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000014; PAS.
DR Pfam; PF00005; ABC_tran; 3.
DR SMART; SM00382; AAA; 2.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 3: Inferred from homology;
KW Antibiotic resistance; ATP-binding; Nucleotide-binding; Plasmid; Repeat.
FT CHAIN 1..488
FT /note="Erythromycin resistance ATP-binding protein MsrA"
FT /id="PRO_0000092614"
FT DOMAIN 6..199
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 299..487
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 200..298
FT /note="Q-linker, rich in Glu and hydrophilic AA"
FT REGION 211..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 211..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 331..338
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 488 AA; 55912 MW; B6F8DA209524510C CRC64;
MEQYTIKFNQ INHKLTDLRS LNIDHLYAYQ FEKIALIGGN GTGKTTLLNM IAQKTKPESG
TVETNGEIQY FEQLNMDVEN DFNTLDGSLM SELHIPMHTT DSMSGGEKAK YKLANVISNY
SPILLLDEPT NHLDKIGKDY LNNILKYYYG TLIIVSHDRA LIDQIADTIW DIQEDGTIRV
FKGNYTQYQN QYEQEQLEQQ RKYEQYISEK QRLSQASKAK RNQAQQMAQA SSKQKNKSIA
PDRLSASKEK GTVEKAAQKQ AKHIEKRMEH LEEVEKPQSY HEFNFPQNKI YDIHNNYPII
AQNLTLVKGS QKLLTQVRFQ IPYGKNIALV GANGVGKTTL LEAIYHQIEG IDCSPKVQMA
YYRQLAYEDM RDVSLLQYLM DETDSSESFS RAILNNLGLN EALERSCNVL SGGERTKLSL
AVLFSTKANM LILDEPTNFL DIKTLEALEM FMNKYPGIIL FTSHDTRFVK HVSDKKWELT
GQSIHDIT
