MACB_SHIFL
ID MACB_SHIFL Reviewed; 648 AA.
AC Q83LR7; Q7C2C3;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 143.
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=SF0839, S0879;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Part of the tripartite efflux system MacAB-TolC. 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:0000255|HAMAP-Rule:MF_01720}.
CC -!- SUBUNIT: Homodimer. Part of the tripartite efflux system MacAB-TolC,
CC which is composed of an inner membrane transporter, MacB, a periplasmic
CC membrane fusion protein, MacA, and an outer membrane component, TolC.
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: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; AE005674; AAN42472.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP16344.1; -; Genomic_DNA.
DR RefSeq; NP_706765.1; NC_004337.2.
DR RefSeq; WP_000188161.1; NZ_WPGW01000037.1.
DR AlphaFoldDB; Q83LR7; -.
DR SMR; Q83LR7; -.
DR STRING; 198214.SF0839; -.
DR EnsemblBacteria; AAN42472; AAN42472; SF0839.
DR EnsemblBacteria; AAP16344; AAP16344; S0879.
DR GeneID; 1023822; -.
DR KEGG; sfl:SF0839; -.
DR KEGG; sft:NCTC1_00837; -.
DR KEGG; sfx:S0879; -.
DR PATRIC; fig|198214.7.peg.968; -.
DR HOGENOM; CLU_000604_78_3_6; -.
DR OMA; VVILITH; -.
DR OrthoDB; 1181903at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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..648
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000269981"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 576..596
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT DOMAIN 5..243
FT /note="ABC transporter"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT BINDING 41..48
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
SQ SEQUENCE 648 AA; 70696 MW; 335792423A0C8586 CRC64;
MTPLLELKDI RRSYPAGDEQ VEVLKGISLN IYAGEMVAIV GASGSGKSTL MNILGCLDKA
TSGTYRVAGQ DIATLDADAL AQLRREHFGF IFQRYHLLPH LTVEQNVEVP AVYAGLERKQ
RLLRAQELLQ RLGLEDRTEY YPAQLSGGQQ QRVSIARALM NGGQVILADE PTGALDSHSG
EEVMAILHQL RDRGHTVIIV THDPQVAAQA ERVIEIRDGE IVRNPPAIEK VNVAGGTEPV
VNTVSGWRQF VSGFNEALTM AWRALAANKM RTLLTMLGII IGIASVVSIV VVGDAAKQMV
LADIRSIGTN TIDVYPGKDF GDDDPQYQQA LKYDDLIAIQ KQPWVASATP AVSQNLRLRY
NNVDVAASAN GVSGDYFNVY GMTFSEGNTF NQEQLNGRAQ VVVLDSNTRR QLFPHKADVV
GEVILVGNMP ARVIGVAEEK QSMFGSSKVL RVWLPYSTMS GRVMGQSWLN SITVRVKEGF
DSAEAEQQLT RLLSLRHGKK DFFTWNMDGV LKTVEKTTRT LQLFLTLVAV ISLVVGGIGV
MNIMLVSVTE RTREIGIRMA VGARASDVLQ QFLIEAVLVC LVGGALGITL SLLIAFTLQL
FLPGWEIGFS PLALLLAFLC STATGILFGW LPARNAARLD PVDALARE
