MACB_CAMJJ
ID MACB_CAMJJ Reviewed; 641 AA.
AC A1VYW8;
DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
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};
GN OrderedLocusNames=CJJ81176_0636;
OS Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=354242;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=81-176;
RA Fouts D.E., Nelson K.E., Sebastian Y.;
RL Submitted (DEC-2006) 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; CP000538; EAQ73027.1; -; Genomic_DNA.
DR RefSeq; WP_002856958.1; NC_008787.1.
DR AlphaFoldDB; A1VYW8; -.
DR SMR; A1VYW8; -.
DR STRING; 354242.CJJ81176_0636; -.
DR EnsemblBacteria; EAQ73027; EAQ73027; CJJ81176_0636.
DR KEGG; cjj:CJJ81176_0636; -.
DR eggNOG; COG0577; Bacteria.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_78_2_7; -.
DR OMA; VVILITH; -.
DR Proteomes; UP000000646; 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..641
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000280165"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 519..539
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 571..591
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 604..624
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT DOMAIN 2..236
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ SEQUENCE 641 AA; 70219 MW; C77C7D6BD7E87863 CRC64;
MIFLKNICKN IGENAILKNV SLSIEKGEFV AIIGQSGSGK TSLLNIIGTL DTPSSGTYVF
DEYEVTKLNN DEKARLRREK IGFIFQRYNL LSLLSAKENV SLPAVYAGKK LQERSQNAKK
LLNDLELAHK LDSKPNELSG GQQQRVSIAR ALMNGGELIL ADEPTGALDS KSGIMVLEIL
QKLNAQGHTI VLVTHDPKIA AQAKRVIEIK DGEILSDTKK EKAQEKLTLK TMSKEKKTLT
LLKNQAFECF KIAYSSILAH KLRSILTMLG IIIGIASVVC VVALGLGSQA KVLESIARLG
TNTIEIRPGR GFGDLRSGKT RLNFSDLETL RSLEYLEAVD AHSNTSGVAT YTNISLSARA
EGVGVNNFAI EGLRIDAGRI LNNDDVKNST NVAVLDFNAK KNLFPDEKSE NILGRVVLFN
SQPFKIIGVL QKDTDKPIED NVVRLYIPYT TLMNKLTGDR NLREIIVKVK DDVSSTLAEN
AIIRILEIKR GQKDFFTFNS DTFKQAITAN KRTTTILTAC VAVIALIVGG IGVMNIMLVS
VSERTREIGI RMAIGARRED IMMQFLIEAV MICTIGAILG VILSIFVIFA FNTLSTDFPM
ILNAYSVLLG LLSSMFIGVV FGFFPARNAA NLNPISALSK E