MACB_BARQU
ID MACB_BARQU Reviewed; 660 AA.
AC Q6FYL0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=BQ12380;
OS Bartonella quintana (strain Toulouse) (Rochalimaea quintana).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Toulouse;
RX PubMed=15210978; DOI=10.1073/pnas.0305659101;
RA Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H.,
RA Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M.,
RA La Scola B., Holmberg M., Andersson S.G.E.;
RT "The louse-borne human pathogen Bartonella quintana is a genomic derivative
RT of the zoonotic agent Bartonella henselae.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004).
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; BX897700; CAF26697.1; -; Genomic_DNA.
DR RefSeq; WP_011179865.1; NC_005955.1.
DR AlphaFoldDB; Q6FYL0; -.
DR SMR; Q6FYL0; -.
DR STRING; 283165.BQ12380; -.
DR PRIDE; Q6FYL0; -.
DR EnsemblBacteria; CAF26697; CAF26697; BQ12380.
DR KEGG; bqu:BQ12380; -.
DR eggNOG; COG0577; Bacteria.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_78_2_5; -.
DR OMA; NEIGVRM; -.
DR OrthoDB; 1181903at2; -.
DR Proteomes; UP000000597; 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; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..660
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000269922"
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 593..613
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 625..645
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT DOMAIN 10..248
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT BINDING 46..53
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ SEQUENCE 660 AA; 72043 MW; 4F3830E86691962B CRC64;
MRTEQADDVL VLENIVRKFS AGETFVTVLK DINLTIKRGE MVAIVGASGS GKSTLMNILG
CLDRPSSGRY WISGKKTACL SADELSALRR NHFGFIFQRY HLLSELTALG NVEIPAIYAG
CSPQIRKKRA QDLLIRLGMG DRINHRPNQL SGGQQQRVSI ARALMNNAEV ILADEPTGAL
DKKSGQEVLR ILDELHQEGR TIVIVTHDMQ VAERAERIIE ISDGEIIADN VAKVAKTKAK
GQALQGKQNP KNQKTLGFFR SFAERFREAF VMALLAMNAH RMRTFLTMLG VIIGIAAIIA
MVALGTGTRE KILENFKSLG SNTLTILPGK SLSDPQSDKI TSLVEADAEA LSRLPYVSGV
TPQVSASSTV RFGAVEVDAV IVGVGEQFFQ TQGLNAVQGR LFDQKSVRDR AVDLVIEKEA
LSVLFPHSRE SPVGKVVQVG QVPARIVGVI DQQHNGGMSN TLQVYLPYTT VQTRFVGTTQ
VRAITVKIAD DIDSHLAESM VRRFLIMRHG EEDFFIRNSQ LFRDRIMEST HILTLLVSSI
AAISLIVGGI GVMNIMLVTV SERINEIGVR MAVGARQSDI LQQFLIEAIL VCIIGGGVGI
LFGLSIGGLF VLFEAPIHLI YTIDSIIISL TFSTLIGICF GFSPARQASR LDPVVALSRD