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   27-MAR-2024, entry version 112.
DE   RecName: Full=Transport ATP-binding protein AarD;
GN   Name=aarD;
OS   Providencia stuartii.
OC   Bacteria; Pseudomonadota; 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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: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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0042883; P:cysteine transport; IEA:InterPro.
DR   CDD; cd18584; ABC_6TM_AarD_CydD; 1.
DR   Gene3D; 1.20.1560.10; ABC transporter type 1, transmembrane domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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   NCBIfam; TIGR02857; CydD; 1.
DR   PANTHER; PTHR24221; ATP-BINDING CASSETTE SUB-FAMILY B; 1.
DR   PANTHER; PTHR24221:SF261; ATP-BINDING_PERMEASE PROTEIN CYDD; 1.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF90123; ABC transporter transmembrane region; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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
//