Y1866_STAAM
ID Y1866_STAAM Reviewed; 578 AA.
AC Q99T13;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Putative multidrug export ATP-binding/permease protein SAV1866;
DE EC=7.6.2.-;
GN OrderedLocusNames=SAV1866;
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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH ADP, FUNCTION,
RP ACTIVITY REGULATION, SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=16943773; DOI=10.1038/nature05155;
RA Dawson R.J.P., Locher K.P.;
RT "Structure of a bacterial multidrug ABC transporter.";
RL Nature 443:180-185(2006).
CC -!- FUNCTION: May be involved in multidrug export. Transmembrane domains
CC (TMD) form a pore in the cell membrane and the ATP-binding domain (NBD)
CC is responsible for energy generation. {ECO:0000269|PubMed:16943773}.
CC -!- ACTIVITY REGULATION: ATPase activity is inhibited by orthovanadate and
CC activated by the cancer drugs doxorubicin and vinblastine.
CC {ECO:0000269|PubMed:16943773}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16943773}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16943773};
CC Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441,
CC ECO:0000269|PubMed:16943773}.
CC -!- DOMAIN: The ATP-binding domain (NBD) and the transmembrane domain (TMD)
CC are fused.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; BA000017; BAB58028.1; -; Genomic_DNA.
DR RefSeq; WP_000597238.1; NC_002758.2.
DR PDB; 2HYD; X-ray; 3.00 A; A/B=1-578.
DR PDB; 2ONJ; X-ray; 3.40 A; A/B=1-578.
DR PDB; 4A82; EM; 2.00 A; A/B/C/D=1-578.
DR PDBsum; 2HYD; -.
DR PDBsum; 2ONJ; -.
DR PDBsum; 4A82; -.
DR AlphaFoldDB; Q99T13; -.
DR SMR; Q99T13; -.
DR DIP; DIP-60414N; -.
DR PaxDb; Q99T13; -.
DR EnsemblBacteria; BAB58028; BAB58028; SAV1866.
DR KEGG; sav:SAV1866; -.
DR HOGENOM; CLU_000604_84_3_9; -.
DR OMA; TMTERFN; -.
DR PhylomeDB; Q99T13; -.
DR BioCyc; SAUR158878:SAV_RS10215-MON; -.
DR BRENDA; 7.6.2.2; 3352.
DR EvolutionaryTrace; Q99T13; -.
DR Proteomes; UP000002481; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..578
FT /note="Putative multidrug export ATP-binding/permease
FT protein SAV1866"
FT /id="PRO_0000271549"
FT TOPO_DOM 1..15
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 37..59
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 81..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 160..162
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 184..244
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..263
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 264..269
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 270..287
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TOPO_DOM 288..578
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 16..306
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 340..575
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 374..381
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT HELIX 2..9
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 10..12
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:4A82"
FT TURN 25..27
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 28..44
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 52..72
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 74..106
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 109..113
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 117..130
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 132..136
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 137..141
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 142..159
FT /evidence="ECO:0007829|PDB:4A82"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 170..215
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 219..272
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 277..285
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 287..290
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 293..318
FT /evidence="ECO:0007829|PDB:4A82"
FT STRAND 340..347
FT /evidence="ECO:0007829|PDB:4A82"
FT STRAND 351..353
FT /evidence="ECO:0007829|PDB:4A82"
FT STRAND 356..364
FT /evidence="ECO:0007829|PDB:4A82"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 380..384
FT /evidence="ECO:0007829|PDB:4A82"
FT TURN 385..389
FT /evidence="ECO:0007829|PDB:4A82"
FT STRAND 394..400
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 410..415
FT /evidence="ECO:0007829|PDB:4A82"
FT STRAND 417..420
FT /evidence="ECO:0007829|PDB:4A82"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 431..435
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 444..453
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 457..461
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 480..494
FT /evidence="ECO:0007829|PDB:4A82"
FT STRAND 497..503
FT /evidence="ECO:0007829|PDB:4A82"
FT TURN 504..507
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 510..523
FT /evidence="ECO:0007829|PDB:4A82"
FT TURN 524..526
FT /evidence="ECO:0007829|PDB:4A82"
FT STRAND 527..532
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 536..538
FT /evidence="ECO:0007829|PDB:4A82"
FT TURN 539..541
FT /evidence="ECO:0007829|PDB:4A82"
FT STRAND 543..549
FT /evidence="ECO:0007829|PDB:4A82"
FT STRAND 552..557
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 559..564
FT /evidence="ECO:0007829|PDB:4A82"
FT HELIX 568..573
FT /evidence="ECO:0007829|PDB:4A82"
FT TURN 574..577
FT /evidence="ECO:0007829|PDB:4A82"
SQ SEQUENCE 578 AA; 64863 MW; 0DA5945AE8F1799C CRC64;
MIKRYLQFVK PYKYRIFATI IVGIIKFGIP MLIPLLIKYA IDGVINNHAL TTDEKVHHLT
IAIGIALFIF VIVRPPIEFI RQYLAQWTSN KILYDIRKKL YNHLQALSAR FYANNQVGQV
ISRVINDVEQ TKDFILTGLM NIWLDCITII IALSIMFFLD VKLTLAALFI FPFYILTVYV
FFGRLRKLTR ERSQALAEVQ GFLHERVQGI SVVKSFAIED NEAKNFDKKN TNFLTRALKH
TRWNAYSFAA INTVTDIGPI IVIGVGAYLA ISGSITVGTL AAFVGYLELL FGPLRRLVAS
FTTLTQSFAS MDRVFQLIDE DYDIKNGVGA QPIEIKQGRI DIDHVSFQYN DNEAPILKDI
NLSIEKGETV AFVGMSGGGK STLINLIPRF YDVTSGQILI DGHNIKDFLT GSLRNQIGLV
QQDNILFSDT VKENILLGRP TATDEEVVEA AKMANAHDFI MNLPQGYDTE VGERGVKLSG
GQKQRLSIAR IFLNNPPILI LDEATSALDL ESESIIQEAL DVLSKDRTTL IVAHRLSTIT
HADKIVVIEN GHIVETGTHR ELIAKQGAYE HLYSIQNL
