MACB_NEIG1
ID MACB_NEIG1 Reviewed; 644 AA.
AC Q5F6V6;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=NGO1439;
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090;
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) 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; AE004969; AAW90081.1; -; Genomic_DNA.
DR RefSeq; WP_003697391.1; NC_002946.2.
DR RefSeq; YP_208493.1; NC_002946.2.
DR AlphaFoldDB; Q5F6V6; -.
DR SMR; Q5F6V6; -.
DR STRING; 242231.NGO_1439; -.
DR PRIDE; Q5F6V6; -.
DR EnsemblBacteria; AAW90081; AAW90081; NGO_1439.
DR KEGG; ngo:NGO_1439; -.
DR PATRIC; fig|242231.10.peg.1697; -.
DR HOGENOM; CLU_000604_78_1_4; -.
DR OMA; VVILITH; -.
DR Proteomes; UP000000535; 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; Reference proteome; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..644
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000269948"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 524..544
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 574..594
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 607..627
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
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"
SQ SEQUENCE 644 AA; 69355 MW; 04F8B662795298D5 CRC64;
MSLIECKNIN RCFGSGENRV HILKDISLSI EKGDFVAIIG QSGSGKSTLM NILGCLDTAG
SGSYRIDGIE TAKMQPDELA ALRRERFGFI FQRYNLLSSL TARDNVALPA VYMGMGGKER
SARADKLLQD LGLASKEGNK PGELSGGQQQ RVSIARALMN GGEIIFADEP TGALDTASGK
NVMEIIRRLH EAGHTVIMVT HDPGIAANAN RVIEIRDGEI ISDTSKNPEI PASNVGRIRE
KASWSFYYDQ FVEAFRMSVQ AVLAHKMRSL LTMLGIIIGI ASVVSVVALG NGSQKKILED
ISSMGTNTIS IFPGRGFGDR RSGKIKTLTI DDAKIIAKQS YVASATPMTS SGGTLTYRNT
DLTASLYGVG EQYFDVRGLK LETGRLFDEN DVKEDAQVVV IDQNVKDKLF ADSDPLGKTI
LFRKRPLTVI GVMKKDENAF GNSDVLMLWS PYTTVMHQIT GESHTNSITV KIKDNANTRV
AEKGLAELLK ARHGTEDFFM NNSDSIRQMV ESTTGTMKLL ISSIALISLV VGGIGVMNIM
LVSVTERTKE IGIRMAIGAR RGNILQQFLI EAVLICIIGG LVGVGLSAAV SLVFNHFVTD
FPMDISAASV IGAVACSTGI GIAFGFMPAN KAAKLNPIDA LAQD