ID Q9AQH1_PSEAI Unreviewed; 574 AA. AC Q9AQH1; DT 01-JUN-2001, integrated into UniProtKB/TrEMBL. DT 01-JUN-2001, sequence version 1. DT 12-APR-2017, entry version 81. DE SubName: Full=ABC transporter {ECO:0000313|EMBL:AAK01462.1}; GN Name=pchI {ECO:0000313|EMBL:AAK01462.1}; OS Pseudomonas aeruginosa. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=287 {ECO:0000313|EMBL:AAK01462.1}; RN [1] {ECO:0000313|EMBL:AAK01462.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PAO1 {ECO:0000313|EMBL:AAK01462.1}; RX PubMed=9846750; RA Reimmann C., Serino L., Beyeler M., Haas D.; RT "Dihydroaeruginoic acid synthetase and pyochelin synthetase, products RT of the pchEF genes, are induced by extracellular pyochelin in RT Pseudomonas aeruginosa."; RL Microbiology 144:3135-3148(1998). RN [2] {ECO:0000313|EMBL:AAK01462.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=PAO1 {ECO:0000313|EMBL:AAK01462.1}; RX PubMed=11208777; DOI=10.1128/JB.183.3.813-820.2001; RA Reimmann C., Patel H.M., Serino L., Barone M., Walsh C.T., Haas D.; RT "Essential PchG-dependent reduction in pyochelin biosynthesis of RT Pseudomonas aeruginosa."; RL J. Bacteriol. 183:813-820(2001). 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; AF074705; AAK01462.1; -; Genomic_DNA. DR ProteinModelPortal; Q9AQH1; -. DR STRING; 208964.PA4222; -. DR PaxDb; Q9AQH1; -. DR eggNOG; ENOG4108K91; Bacteria. DR eggNOG; COG1132; LUCA. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042626; F:ATPase activity, coupled to transmembrane movement of substances; IEA:InterPro. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011527; ABC1_TM_dom. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. 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 4: Predicted; KW ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00434}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00434}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 21 42 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 54 75 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 129 148 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 154 173 Helical. {ECO:0000256|SAM:Phobius}. FT TRANSMEM 239 259 Helical. {ECO:0000256|SAM:Phobius}. FT DOMAIN 21 291 ABC transmembrane type-1. FT {ECO:0000259|PROSITE:PS50929}. FT DOMAIN 328 562 ABC transporter. {ECO:0000259|PROSITE: FT PS50893}. FT NP_BIND 361 368 ATP. {ECO:0000256|PROSITE-ProRule: FT PRU00434}. SQ SEQUENCE 574 AA; 61407 MW; 89762C4FE0481D8B CRC64; MTLFERMRAL PEDCRAALRR ASAWAVLAAL LDAACGVLLV PLVEAWFAEG ALPWRWVAAL LGLSLAQALL QYLALRRGFA AGGSLAAGLV RSLVARLPRL APPALRRVAP AEGLLRGPVM QAMGIPAHLL GPLIAALVTP LGVILGLFLI DPSIALGLLL AGAFLAALLR WSGRRNLAAE DARLAAERDA ARQLQAFAER QPLLRAAQRE SVARQGLEEA LRSLHRSTLD LLRRSLPSGL GFALAVQAAF AFALLGGAWA VERQWLDGAR LVAVLVLLVR FIEPLAQLTH LDQALRGAWQ ALDTLLRVFA LAPLRSPEPG ERPHDASLAA EAVELRLEDG RALLEDISLR LEPGSLNVLV GPSGAGKSSL LALLGRLYDV DAGRVLLGGV DIRRLSETTL AASRNLVFQD NGLFRGSVAW NLRMARADAD LEALREAARA VGLLEEIEAW PQGWDSDVGP GGALLSGGQR QRLCLARGLL STAPLLLLDE PTASLDAASE AQVLRSLLGL RGRRTLLVLT HRPALARQAD QVLLLEEGRL RLSGLHADLL VRDDWYAGFV GLAGEESSAT VVDR //