MACB_BARHE
ID MACB_BARHE Reviewed; 660 AA.
AC Q6G1V5;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=BH15460;
OS Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
OS (Rochalimaea henselae).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=283166;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49882 / DSM 28221 / Houston 1;
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; BX897699; CAF28309.1; -; Genomic_DNA.
DR RefSeq; WP_011181312.1; NZ_LRIJ02000001.1.
DR AlphaFoldDB; Q6G1V5; -.
DR SMR; Q6G1V5; -.
DR STRING; 283166.BH15460; -.
DR PaxDb; Q6G1V5; -.
DR PRIDE; Q6G1V5; -.
DR EnsemblBacteria; CAF28309; CAF28309; BH15460.
DR GeneID; 64157685; -.
DR KEGG; bhe:BH15460; -.
DR eggNOG; COG0577; Bacteria.
DR eggNOG; COG1136; Bacteria.
DR OMA; NEIGVRM; -.
DR Proteomes; UP000000421; 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_0000269921"
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; 72232 MW; 440391550AF991B4 CRC64;
MKAKQADAVL VLENIVRKFP AGETFVTVLK DINLTIKRGE MVAIVGASGS GKSTLMNILG
CLDRPTFGRY WISGKETASL SADELSALRR NHFGFIFQRY HLLNELTALG NVEIPAVYAG
YAPEVRRKRA EDLLTRLGMR DRIHHRPNQL SGGQQQRVSI ARALMNNAEV ILADEPTGAL
DKKSGQEVLR ILDELHQEGR TIIMVTHDMQ VAERADRIIE ISDGEIIADN VSKVAKTKTD
SQALYGKQVL KDQKTLGFFR SFAERFREAF VMALLAMNAH RMRTFLTMLG VIIGIGAIIA
MVALGNGTRE KILENFKSLG SNTLTILPGK SLSDPQAEKI TSLVEADAEA LSKLPYVSGV
TPQMSASSTI RFGSVEADVV IAGVGEQYFQ TQGLNAVQGR LFDQKSVHDR AIDLVIEKEA
LAVLFPHSHE SPLGKVVHVG NVPVRIVGVI DPQHNGGTSS TLQVYLPYTT VQTRFLGTTQ
VRAITVKIAD TVDSNLAETM VRRFLIMRHG EEDFFIRNSQ LFRDRIMEST HILTLLVSSI
AAISLIVGGI GVMNIMLVTV SERINEIGVR MAVGARQSDI LQQFLIEAIL VCVIGGGLGI
LFGMSIGGLF LLFKAPIHLI YTIDSIILSL TFSTLIGVCF GFSPARQASR LDPVVALSRD