MACB_AGGAC
ID MACB_AGGAC Reviewed; 644 AA.
AC Q2EHL8;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 82.
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, ECO:0000303|PubMed:17116373};
OS Aggregatibacter actinomycetemcomitans (Actinobacillus
OS actinomycetemcomitans) (Haemophilus actinomycetemcomitans).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Aggregatibacter.
OX NCBI_TaxID=714;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=IDH781;
RX PubMed=17116373; DOI=10.1016/j.gene.2006.10.004;
RA Crosby J.A., Kachlany S.C.;
RT "TdeA, a TolC-like protein required for toxin and drug export in
RT Aggregatibacter (Actinobacillus) actinomycetemcomitans.";
RL Gene 388:83-92(2007).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 293-518, FUNCTION, AND SUBUNIT.
RX PubMed=19432486; DOI=10.1021/bi900415t;
RA Xu Y., Sim S.H., Nam K.H., Jin X.L., Kim H.M., Hwang K.Y., Lee K., Ha N.C.;
RT "Crystal structure of the periplasmic region of MacB, a noncanonic ABC
RT transporter.";
RL Biochemistry 48:5218-5225(2009).
CC -!- FUNCTION: Part of the tripartite efflux system MacAB-TdeA. 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:0000303|PubMed:19432486}.
CC -!- SUBUNIT: Homodimer. Part of the tripartite efflux system MacAB-TdeA,
CC which is composed of an inner membrane transporter, MacB, a periplasmic
CC membrane fusion protein, MacA, and an outer membrane component, TdeA.
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:0000303|PubMed:19432486}.
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 -!- DISRUPTION PHENOTYPE: Mutation does not produce a noticeable phenotype
CC or alter the drug resistance profile and the hemolytic activity of
CC A.actinomycetemcomitans. {ECO:0000269|PubMed:17116373}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Macrolide
CC exporter (TC 3.A.1.122) family. {ECO:0000255|HAMAP-Rule:MF_01720}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD38132.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ378165; ABD38132.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_025298382.1; NZ_CP065604.1.
DR PDB; 3FTJ; X-ray; 2.00 A; A=293-518.
DR PDB; 5LIL; X-ray; 3.35 A; A/B=1-644.
DR PDB; 5LJ6; X-ray; 3.90 A; A=1-644.
DR PDB; 5LJ7; X-ray; 3.25 A; A/B=1-644.
DR PDBsum; 3FTJ; -.
DR PDBsum; 5LIL; -.
DR PDBsum; 5LJ6; -.
DR PDBsum; 5LJ7; -.
DR AlphaFoldDB; Q2EHL8; -.
DR SMR; Q2EHL8; -.
DR STRING; 714.ACT75_10875; -.
DR TCDB; 3.A.1.122.35; the atp-binding cassette (abc) superfamily.
DR PRIDE; Q2EHL8; -.
DR eggNOG; COG0577; Bacteria.
DR eggNOG; COG1136; Bacteria.
DR EvolutionaryTrace; Q2EHL8; -.
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 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; ATP-binding; Cell inner membrane;
KW Cell membrane; Membrane; Nucleotide-binding; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..644
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000269917"
FT TOPO_DOM 1..268
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P75831, ECO:0000305"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TOPO_DOM 290..523
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P75831, ECO:0000305"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TOPO_DOM 545..573
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P75831, ECO:0000305"
FT TRANSMEM 574..594
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TOPO_DOM 595..607
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P75831, ECO:0000305"
FT TRANSMEM 608..628
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TOPO_DOM 629..644
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P75831, ECO:0000305"
FT DOMAIN 4..242
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT STRAND 2..14
FT /evidence="ECO:0007829|PDB:5LJ7"
FT STRAND 20..31
FT /evidence="ECO:0007829|PDB:5LJ7"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:5LJ7"
FT HELIX 46..53
FT /evidence="ECO:0007829|PDB:5LJ7"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:5LJ7"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:5LJ7"
FT HELIX 76..85
FT /evidence="ECO:0007829|PDB:5LJ7"
FT STRAND 87..90
FT /evidence="ECO:0007829|PDB:5LJ7"
FT HELIX 102..111
FT /evidence="ECO:0007829|PDB:5LJ7"
FT TURN 112..114
FT /evidence="ECO:0007829|PDB:5LJ7"
FT HELIX 117..130
FT /evidence="ECO:0007829|PDB:5LJ7"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:5LJ7"
FT HELIX 141..143
FT /evidence="ECO:0007829|PDB:5LJ7"
FT HELIX 146..157
FT /evidence="ECO:0007829|PDB:5LJ7"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:5LJ7"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:5LJ7"
FT TURN 170..173
FT /evidence="ECO:0007829|PDB:5LJ7"
FT HELIX 176..191
FT /evidence="ECO:0007829|PDB:5LJ7"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:5LJ7"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:5LJ7"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:5LJ7"
FT STRAND 219..227
FT /evidence="ECO:0007829|PDB:5LJ7"
FT HELIX 247..263
FT /evidence="ECO:0007829|PDB:5LJ7"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:3FTJ"
FT STRAND 303..314
FT /evidence="ECO:0007829|PDB:3FTJ"
FT HELIX 319..323
FT /evidence="ECO:0007829|PDB:3FTJ"
FT HELIX 329..336
FT /evidence="ECO:0007829|PDB:3FTJ"
FT STRAND 341..356
FT /evidence="ECO:0007829|PDB:3FTJ"
FT STRAND 359..369
FT /evidence="ECO:0007829|PDB:3FTJ"
FT HELIX 373..377
FT /evidence="ECO:0007829|PDB:3FTJ"
FT STRAND 381..384
FT /evidence="ECO:0007829|PDB:3FTJ"
FT HELIX 389..394
FT /evidence="ECO:0007829|PDB:3FTJ"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:3FTJ"
FT HELIX 403..410
FT /evidence="ECO:0007829|PDB:3FTJ"
FT STRAND 419..422
FT /evidence="ECO:0007829|PDB:3FTJ"
FT STRAND 425..433
FT /evidence="ECO:0007829|PDB:3FTJ"
FT STRAND 447..451
FT /evidence="ECO:0007829|PDB:3FTJ"
FT HELIX 452..458
FT /evidence="ECO:0007829|PDB:3FTJ"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:3FTJ"
FT STRAND 466..472
FT /evidence="ECO:0007829|PDB:3FTJ"
FT STRAND 474..476
FT /evidence="ECO:0007829|PDB:5LJ7"
FT HELIX 478..493
FT /evidence="ECO:0007829|PDB:3FTJ"
FT STRAND 498..502
FT /evidence="ECO:0007829|PDB:3FTJ"
FT HELIX 503..511
FT /evidence="ECO:0007829|PDB:3FTJ"
FT HELIX 548..556
FT /evidence="ECO:0007829|PDB:5LJ7"
FT HELIX 561..597
FT /evidence="ECO:0007829|PDB:5LJ7"
FT HELIX 609..633
FT /evidence="ECO:0007829|PDB:5LJ7"
FT HELIX 637..641
FT /evidence="ECO:0007829|PDB:5LJ7"
SQ SEQUENCE 644 AA; 69871 MW; BA25F3FF3E002234 CRC64;
MNIIEIKQLN RYFGEGENRV HVLKDISLSI ERGDFVAIMG QSGSGKSTLM NIIGCLDTAT
GGSSKIDGKE TIELTNDQLS DLRSQKFGFI FQRYNLLSSL TAAENVALPA IYAGMPQSQR
LERAKQLLEK LGLGDKWQNK PNQLSGGQQQ RVSIARALMN GGEIILADEP TGALDSHSGE
NVMEILRQLH EEGHTIIMVT HDKHIAASAN RIIEIKDGEI ISDTQKRQVK SAVKNPSVFK
GRFGFSKDQL MEAFRMSVSA IVAHKMRSLL TMLGIIIGIT SVVSVVALGN GSQQKILENI
RGIGTNTMTI FNGNGFGDRR SRHIQNLKIS DANTLSKQSY IQSVTPNTSS SGILVVGNKS
FTSANLYGIG EQYFDVEGLK LKQGRLLTED DVDQSNQVVV LDESAKKAIF ANENPLGKTV
IFNKRPFRVI GVVSDQQLGG FPGNSLNLYS PYSTVLNKIT GGSRIGSITV KISDDVNSTV
AEKSLTELLK SLHGKKDFFI MNSDTIKQTI ENTTGTMKLL ISSIAFISLI VGGIGVMNIM
LVSVTERTKE IGVRMAIGAR QINILQQFLI EAVLICLIGG VAGILLSVLI GVLFNSFITD
FSMDFSTASI VTAVLFSTLI GVLFGYMPAK KAAELNPITA LAQE
