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MACB2_PSEF5
ID   MACB2_PSEF5             Reviewed;         657 AA.
AC   Q4K9A4;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Macrolide export ATP-binding/permease protein MacB 2 {ECO:0000255|HAMAP-Rule:MF_01720};
DE            EC=7.6.2.- {ECO:0000255|HAMAP-Rule:MF_01720};
GN   Name=macB2 {ECO:0000255|HAMAP-Rule:MF_01720}; OrderedLocusNames=PFL_4082;
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
CC   -!- FUNCTION: Part of the tripartite efflux system MacAB-TolC. MacB is a
CC       non-canonical ABC transporter that contains transmembrane domains
CC       (TMD), which form a pore in the inner membrane, and an ATP-binding
CC       domain (NBD), which is responsible for energy generation. Confers
CC       resistance against macrolides. {ECO:0000255|HAMAP-Rule:MF_01720}.
CC   -!- SUBUNIT: Homodimer. Part of the tripartite efflux system MacAB-TolC,
CC       which is composed of an inner membrane transporter, MacB, a periplasmic
CC       membrane fusion protein, MacA, and an outer membrane component, TolC.
CC       The complex forms a large protein conduit and can translocate molecules
CC       across both the inner and outer membranes. Interacts with MacA.
CC       {ECO:0000255|HAMAP-Rule:MF_01720}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01720}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01720}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Macrolide
CC       exporter (TC 3.A.1.122) family. {ECO:0000255|HAMAP-Rule:MF_01720}.
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DR   EMBL; CP000076; AAY93343.1; -; Genomic_DNA.
DR   RefSeq; WP_011062363.1; NC_004129.6.
DR   AlphaFoldDB; Q4K9A4; -.
DR   SMR; Q4K9A4; -.
DR   STRING; 220664.PFL_4082; -.
DR   EnsemblBacteria; AAY93343; AAY93343; PFL_4082.
DR   KEGG; pfl:PFL_4082; -.
DR   PATRIC; fig|220664.5.peg.4181; -.
DR   eggNOG; COG0577; Bacteria.
DR   eggNOG; COG1136; Bacteria.
DR   HOGENOM; CLU_000604_78_2_6; -.
DR   OMA; VVILITH; -.
DR   OrthoDB; 1181903at2; -.
DR   Proteomes; UP000008540; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   CDD; cd03255; ABC_MJ0796_LolCDE_FtsE; 1.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003838; ABC3_permease_dom.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR017911; MacB_ATP-bd.
DR   InterPro; IPR025857; MacB_PCD.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 1.
DR   Pfam; PF02687; FtsX; 1.
DR   Pfam; PF12704; MacB_PCD; 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;
KW   Antibiotic resistance; ATP-binding; Cell inner membrane; Cell membrane;
KW   Membrane; Nucleotide-binding; Reference proteome; Translocase;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..657
FT                   /note="Macrolide export ATP-binding/permease protein MacB
FT                   2"
FT                   /id="PRO_0000269958"
FT   TRANSMEM        285..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        532..552
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        590..610
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   TRANSMEM        620..640
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   DOMAIN          6..245
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT   BINDING         43..50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ   SEQUENCE   657 AA;  69771 MW;  86ABF5699B8819E6 CRC64;
     MQTPLIDLRN IRKSYGGGDS PQVDVLRGID LSIHAGEFVA IVGASGSGKS TLMNILGCLD
     RPTSGEYLFA GENVAHLDSD ELAWLRREAF GFVFQGYHLI PSASAQENVE MPAIYAGTPT
     AERHTRAAAL LERLGLASRS GNRPHQLSGG QQQRVSIARA LMNGGHIILA DEPTGALDSH
     SGAEVMALLD ELASQGHVVI LITHDREVAA RAKRIIEIRD GEIISDTATS DPSVQLSANA
     GALQAVDLRQ RLADGSEPTG AWKGELLEAI QAAWRVMWIN RFRTALTLLG IIIGVASVVV
     MLAVGEGSKR QVMAQMGAFG SNIIYLSGYS PNPRTPEGIV TLDDVAALAN LPQVKRIMAV
     NGAKAGVRFG NADYMSYVGG NDTNFPEIFN WPVAQGSYFS EADESSAAAV AVIGHKVREK
     LLKDVANPIG QYILIENVPF QVVGVLSEKG ASSGDSDSDD RIAVPYSAAS IRLFGDHNPQ
     YVAIAAADAS RVKQTEQEID ELMLRMHGGK RDFELTNNAA MIQAEARTQN TLSLMLGAIA
     AISLLVGGIG VMNIMLMTVR ERTREIGIRM ATGARQRDIL RQFLTEAVML SVVGGLAGIG
     VALIIGGILI LSEVAVAFSL AAVLGAFACA LVTGVIFGFM PARKAARLDP VTALTSE
 
 
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