MACB_CHLCH
ID MACB_CHLCH Reviewed; 657 AA.
AC Q3ATR5;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Macrolide export ATP-binding/permease protein MacB {ECO:0000255|HAMAP-Rule:MF_01720};
DE EC=7.6.2.- {ECO:0000255|HAMAP-Rule:MF_01720};
GN Name=macB {ECO:0000255|HAMAP-Rule:MF_01720}; OrderedLocusNames=Cag_0337;
OS Chlorobium chlorochromatii (strain CaD3).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=340177;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CaD3;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Chlorobium chlorochromatii CaD3.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Non-canonical ABC transporter that contains transmembrane
CC domains (TMD), which form a pore in the inner membrane, and an ATP-
CC binding domain (NBD), which is responsible for energy generation.
CC Confers resistance against macrolides. {ECO:0000255|HAMAP-
CC Rule:MF_01720}.
CC -!- SUBUNIT: Homodimer. {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; CP000108; ABB27610.1; -; Genomic_DNA.
DR RefSeq; WP_011361383.1; NC_007514.1.
DR AlphaFoldDB; Q3ATR5; -.
DR SMR; Q3ATR5; -.
DR STRING; 340177.Cag_0337; -.
DR EnsemblBacteria; ABB27610; ABB27610; Cag_0337.
DR KEGG; cch:Cag_0337; -.
DR eggNOG; COG0577; Bacteria.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_78_2_10; -.
DR OMA; VVILITH; -.
DR OrthoDB; 1181903at2; -.
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; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..657
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000269935"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 533..553
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 591..611
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 5..244
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT BINDING 41..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ SEQUENCE 657 AA; 70936 MW; 4C9C57587544BA4A CRC64;
MSALLELVDV QRSYTIGESE VAALRGVSLT IERGEFVAIM GASGSGKSSL LHILGLLDTP
DKGSYRIAGS DVATLSDDAR ASLRNHVAGF VFQQFHLLRR MSIEDNVRLP MLYSGVERSS
NLQAEAIRRL EMVGLAHRLH HTPSQLSGGE QQRVAIARAL IRQPAIIFAD EPTGNLDTRN
SLEIMKILQG LHEEGKTIVM VTHEPDIAAY ADRIITMRDG VIISDERKAT ATVLPSSDSP
FVLPTTAIAA WWHYKRLSGF VAQAMQAILA NKMRSLLSML GILVGVASVI AMMALGEGAR
VAMQEELKAM GSNMLSVRGG SAKIRGTSQG AGAVTRFTVK DVEAIAALRP LVRNASGVVN
GSARVVYGNR NWSSSLLGAG YDYGTMRAAL PTVGRWFTAE ELQRRDKVAI IGVTVARELF
GESNPLGKTI KINRINFTVI GLAPAKGFVG PQDEDDIVMI PLSTAMYRVL GRDYLSGIFV
EVAEAHRVDE ARQRIAAFIR QRHRLPVDDD SFYIRDMTEI QKMLSSTTRT MSLLLGAIAA
ISLVVGGIGI MNIMLVSVTE RTREIGLRKA LGARNSDIML QFLVESAGMT LLGGVLGLLV
GIGVALGLTL VAGWAVKISL FSVLLATLFS AVTGLFFGLW PAQKAAALKP VEALRYE