ID MDLA_ECOLI Reviewed; 590 AA.
AC P77265; P30751; Q2MBX8;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 02-NOV-2016, entry version 141.
DE RecName: Full=Multidrug resistance-like ATP-binding protein MdlA;
DE EC=3.6.3.44;
GN Name=mdlA; Synonyms=mdl; OrderedLocusNames=b0448, JW0438;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TAP90 / ATCC 47037;
RX PubMed=7904973; DOI=10.1016/0378-1119(93)90470-N;
RA Allikmets R., Gerrard B.C., Court D., Dean M.C.;
RT "Cloning and organization of the abc and mdl genes of Escherichia
RT coli: relationship to eukaryotic multidrug resistance.";
RL Gene 136:231-236(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA Mau B., Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains
RT MG1655 and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + xenobiotic(In) = ADP + phosphate
CC + xenobiotic(Out).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255|PROSITE-ProRule:PRU00441,
CC ECO:0000269|PubMed:15919996}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Drug
CC exporter-2 (TC 3.A.1.117) family. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- SIMILARITY: Contains 1 ABC transporter domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00434}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC36870.1; Type=Frameshift; Positions=546; Note=Fuses together mdlA and mdlB.; Evidence={ECO:0000305};
DR EMBL; L08627; AAC36870.1; ALT_FRAME; Unassigned_DNA.
DR EMBL; U82664; AAB40204.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73551.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76228.1; -; Genomic_DNA.
DR PIR; H64774; H64774.
DR RefSeq; NP_414982.1; NC_000913.3.
DR RefSeq; WP_001235649.1; NZ_LN832404.1.
DR ProteinModelPortal; P77265; -.
DR SMR; P77265; -.
DR BioGrid; 4261677; 138.
DR DIP; DIP-10173N; -.
DR IntAct; P77265; 1.
DR STRING; 511145.b0448; -.
DR TCDB; 3.A.1.106.13; the atp-binding cassette (abc) superfamily.
DR PaxDb; P77265; -.
DR PRIDE; P77265; -.
DR EnsemblBacteria; AAC73551; AAC73551; b0448.
DR EnsemblBacteria; BAE76228; BAE76228; BAE76228.
DR GeneID; 945092; -.
DR KEGG; ecj:JW0438; -.
DR KEGG; eco:b0448; -.
DR PATRIC; 32116049; VBIEscCol129921_0466.
DR EchoBASE; EB1579; -.
DR EcoGene; EG11622; mdlA.
DR eggNOG; ENOG4105BZ1; Bacteria.
DR eggNOG; COG1132; LUCA.
DR InParanoid; P77265; -.
DR KO; K18889; -.
DR OMA; SWRYTLG; -.
DR PhylomeDB; P77265; -.
DR BioCyc; EcoCyc:MDLA-MONOMER; -.
DR BioCyc; ECOL316407:JW0438-MONOMER; -.
DR PRO; PR:P77265; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0034040; F:lipid-transporting ATPase activity; IBA:GO_Central.
DR GO; GO:0008559; F:xenobiotic-transporting ATPase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.300; -; 1.
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; 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 3: Inferred from homology;
KW ATP-binding; Cell inner membrane; Cell membrane; Complete proteome;
KW Hydrolase; Membrane; Nucleotide-binding; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1 590 Multidrug resistance-like ATP-binding
FT protein MdlA.
FT /FTId=PRO_0000092492.
FT TRANSMEM 23 43 Helical. {ECO:0000255|PROSITE-
FT ProRule:PRU00441}.
FT TRANSMEM 53 73 Helical. {ECO:0000255|PROSITE-
FT ProRule:PRU00441}.
FT TRANSMEM 134 154 Helical. {ECO:0000255|PROSITE-
FT ProRule:PRU00441}.
FT TRANSMEM 155 175 Helical. {ECO:0000255|PROSITE-
FT ProRule:PRU00441}.
FT TRANSMEM 248 268 Helical. {ECO:0000255|PROSITE-
FT ProRule:PRU00441}.
FT TRANSMEM 280 300 Helical. {ECO:0000255|PROSITE-
FT ProRule:PRU00441}.
FT DOMAIN 18 303 ABC transmembrane type-1.
FT {ECO:0000255|PROSITE-ProRule:PRU00441}.
FT DOMAIN 337 570 ABC transporter. {ECO:0000255|PROSITE-
FT ProRule:PRU00434}.
FT NP_BIND 369 376 ATP. {ECO:0000255|PROSITE-
FT ProRule:PRU00434}.
FT CONFLICT 145 145 G -> A (in Ref. 1; AAC36870).
FT {ECO:0000305}.
FT CONFLICT 234 235 NM -> KL (in Ref. 1; AAC36870).
FT {ECO:0000305}.
FT CONFLICT 318 318 A -> R (in Ref. 1; AAC36870).
FT {ECO:0000305}.
FT CONFLICT 371 371 T -> N (in Ref. 1; AAC36870).
FT {ECO:0000305}.
FT CONFLICT 390 390 E -> P (in Ref. 1; AAC36870).
FT {ECO:0000305}.
FT CONFLICT 410 411 SR -> TG (in Ref. 1; AAC36870).
FT {ECO:0000305}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 352 500 ipfam:ABC_tran [T]
FT MYHIT 361 547 ismart:AAA [T]
FT MYHIT 473 487 ipat:ABC_TRANSPORTER_1 [T]
FT MYHIT 19 303 iprf:ABC_TM1F [T]
FT MYHIT 337 570 iprf:ABC_TRANSPORTER_2 [T]
FT MYHIT 22 291 ipfam:ABC_membrane [T]
SQ SEQUENCE 590 AA; 66017 MW; AD1CEBE41030200D CRC64;
MRLFAQLSWY FRREWRRYLG AVALLVIIAM LQLVPPKVVG IVVDGVTEQH FTTGQILMWI
ATMVLIAVVV YLLRYVWRVL LFGASYQLAV ELREDYYRQL SRQHPEFYLR HRTGDLMARA
TNDVDRVVFA AGEGVLTLVD SLVMGCAVLI MMSTQISWQL TLFSLLPMPV MAIMIKRNGD
ALHERFKLAQ AAFSSLNDRT QESLTSIRMI KAFGLEDRQS ALFAADAEDT GKKNMRVARI
DARFDPTIYI AIGMANLLAI GGGSWMVVQG SLTLGQLTSF MMYLGLMIWP MLALAWMFNI
VERGSAAYSR IRAMLAEAPV VNDGSEPVPE GRGELDVNIH QFTYPQTDHP ALENVNFALK
PGQMLGICGP TGSGKSTLLS LIQRHFDVSE GDIRFHDIPL TKLQLDSWRS RLAVVSQTPF
LFSDTVANNI ALGCPNATQQ EIEHVARLAS VHDDILRLPQ GYDTEVGERG VMLSGGQKQR
ISIARALLVN AEILILDDAL SAVDGRTEHQ ILHNLRQWGQ GRTVIISAHR LSALTEASEI
IVMQHGHIAQ RGNHDVLAQQ SGWYRDMYRY QQLEAALDDA PENREEAVDA
//
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