(data stored in SCRATCH zone)

SWISSPROT: C7QJ24_CATAD

ID   C7QJ24_CATAD            Unreviewed;       256 AA.
AC   C7QJ24;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   07-JUN-2017, entry version 66.
DE   RecName: Full=Macrolide export ATP-binding/permease protein MacB {ECO:0000256|HAMAP-Rule:MF_01720};
DE            EC=3.6.3.- {ECO:0000256|HAMAP-Rule:MF_01720};
GN   Name=macB {ECO:0000256|HAMAP-Rule:MF_01720};
GN   OrderedLocusNames=Caci_0211 {ECO:0000313|EMBL:ACU69166.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69166.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69166.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
CC   -!- FUNCTION: Non-canonical ABC transporter that contains
CC       transmembrane domains (TMD), which form a pore in the membrane,
CC       and an ATP-binding domain (NBD), which is responsible for energy
CC       generation. Confers resistance against macrolides.
CC       {ECO:0000256|HAMAP-Rule:MF_01720}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01720,
CC       ECO:0000256|SAAS:SAAS00548216}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|SAAS:SAAS00355363}; Multi-pass membrane protein
CC       {ECO:0000256|SAAS:SAAS00355363}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01720}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01720}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Macrolide
CC       exporter (TC 3.A.1.122) family. {ECO:0000256|HAMAP-Rule:MF_01720,
CC       ECO:0000256|SAAS:SAAS00548212}.
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DR   EMBL; CP001700; ACU69166.1; -; Genomic_DNA.
DR   STRING; 479433.Caci_0211; -.
DR   EnsemblBacteria; ACU69166; ACU69166; Caci_0211.
DR   KEGG; cai:Caci_0211; -.
DR   eggNOG; ENOG4105D6C; Bacteria.
DR   eggNOG; COG1136; LUCA.
DR   KO; K02003; -.
DR   OMA; ETSYEVM; -.
DR   OrthoDB; POG091H023H; -.
DR   Proteomes; UP000000851; 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:0042895; F:antibiotic transporter activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATPase activity; IEA:InterPro.
DR   GO; GO:0016820; F:hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like.
DR   InterPro; IPR017871; ABC_transporter_CS.
DR   InterPro; IPR017911; ABC_transptr_macrolide_ATP-bd.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR   PROSITE; PS51267; MACB; 1.
PE   3: Inferred from homology;
DR   PRODOM; C7QJ24.
DR   SWISS-2DPAGE; C7QJ24.
KW   Antibiotic resistance {ECO:0000256|HAMAP-Rule:MF_01720,
KW   ECO:0000256|SAAS:SAAS00432892};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01720, ECO:0000256|PROSITE-
KW   ProRule:PRU00434, ECO:0000256|SAAS:SAAS00034249};
KW   Cell inner membrane {ECO:0000256|SAAS:SAAS00034256};
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01720,
KW   ECO:0000256|SAAS:SAAS00034245};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01720,
KW   ECO:0000256|SAAS:SAAS00034244};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01720,
KW   ECO:0000256|SAAS:SAAS00034255};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01720,
KW   ECO:0000256|PROSITE-ProRule:PRU00434, ECO:0000256|SAAS:SAAS00034258};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01720,
KW   ECO:0000256|SAAS:SAAS00034254};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01720,
KW   ECO:0000256|SAAS:SAAS00034252};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01720,
KW   ECO:0000256|SAAS:SAAS00034247}.
FT   DOMAIN       16    256       MACB. {ECO:0000259|PROSITE:PS51267}.
FT   DOMAIN       17    255       ABC transporter. {ECO:0000259|PROSITE:
FT                                PS50893}.
FT   NP_BIND      53     60       ATP. {ECO:0000256|PROSITE-ProRule:
FT                                PRU00434}.
SQ   SEQUENCE   256 AA;  27362 MW;  4BCCAB7EF8786709 CRC64;
     MTGVSGPGGS EGRKPVIELA DIRKTYGMDG TAVHALRGVT LTVPAGDYVA IMGASGSGKS
     TMMNIIGCLD VPTSGRYLLD GIEVEHLSDR QLALVRNRKI GFVFQSFNLL PRTTALDNVE
     LPLIYAGVGT AERRKRARAA LELVGLGDRM NHKPQELSGG QQQRVAVARA LVTAPSLILA
     DEPTGNLDSA SSEDVMALFD RLHQAGRTIV LITHEHDIAE HADRAIRLMD GQIVSDERNG
     ARGWLSAQHS AKHGSA
//

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