AARD_PROST
ID AARD_PROST Reviewed; 588 AA.
AC Q52402;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Transport ATP-binding protein AarD;
GN Name=aarD;
OS Providencia stuartii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=588;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=PR50;
RX PubMed=8830242; DOI=10.1046/j.1365-2958.1996.385912.x;
RA Macinga D.R., Rather P.N.;
RT "aarD, a Providencia stuartii homologue of cydD: role in 2'-N-
RT acetyltransferase expression, cell morphology and growth in the presence of
RT an extracellular factor.";
RL Mol. Microbiol. 19:511-520(1996).
CC -!- FUNCTION: Somehow involved in the cytochrome D branch of aerobic
CC respiration. Seems to be a component of a transport system (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR EMBL; U30383; AAB18930.1; -; Genomic_DNA.
DR PIR; S70900; S70900.
DR AlphaFoldDB; Q52402; -.
DR SMR; Q52402; -.
DR STRING; 588.BGK56_19310; -.
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 GO; GO:0042883; P:cysteine transport; IEA:InterPro.
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; IPR014216; ABC_transptr_CydD.
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 TIGRFAMs; TIGR02857; CydD; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW Nucleotide-binding; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..588
FT /note="Transport ATP-binding protein AarD"
FT /id="PRO_0000091919"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 24..316
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 350..583
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 383..390
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ SEQUENCE 588 AA; 65778 MW; 3CCE18DDA53B7D36 CRC64;
MDKTRQTELV RWLKQHSTSA KRWLRISMLL GVVSGLLIIA QAWFLAVILQ ALIMEHTPRE
QLLTPFILLL AVFVLRALLT VIRERVGFRC GQVVRQEVRN MVLNKLQALG PVWVKGKPAG
SWATIVLEQI EDMQEYYSRY LPQMYLAGII PIMILIAIFP FNWAAALILF ATAPLIPIFM
ALVGLGAADA NRRNFVALGR LSGSFLDRLR GLDTLRLFFR EKAEVQQIRE STEDFRSRTM
EVLRMAFLSS GVLEFFASIS IAIVAVYFGF SYLGELNFGS YGLPVTMFAG FLALILSPEF
FQPLRDLGTY YHAKAQAVGA AESLVTLLES DGEQKTETGD KTPQDKPIQI EANKLEIYSH
DGQRLVGPLD FTIEPQQRIA VFGQSGAGKS SLLNLLLGFL PYKGSIKING DELKELCPDK
WRALIGWVGQ NPHLPEQTLI ENICLGKPTA SEAEIQQAID DAYVSEFLPM LPDGLNTRLG
DYAARLSVGQ AQRVAVARTL LKPSRILLLD EPAASLDAHS EKRVMHTLNQ LAQQQTTIMV
THLLEETVNY DQIWVMANGQ IIQRGHYAQL SQSEGPFARL LAHRSEEL