ID   MACA_SHIFL              Reviewed;         371 AA.
AC   P64177; P58410;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 108.
DE   RecName: Full=Macrolide export protein MacA;
GN   Name=macA; OrderedLocusNames=SF0838, S0878;
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. MacA
CC       stimulates the ATPase activity of MacB by promoting the closed ATP-
CC       bound state of MacB, increases the capacity of MacB to bind macrolides
CC       such as erythromycin, and provides a physical link between MacB and
CC       TolC. Confers resistance against macrolides (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homohexamer. 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. MacA interacts with MacB and
CC       TolC (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}; Periplasmic side {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC       family. {ECO:0000305}.
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DR   EMBL; AE005674; AAN42471.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP16343.1; -; Genomic_DNA.
DR   RefSeq; NP_706764.2; NC_004337.2.
DR   RefSeq; WP_000746446.1; NZ_WPGW01000037.1.
DR   AlphaFoldDB; P64177; -.
DR   SMR; P64177; -.
DR   STRING; 198214.SF0838; -.
DR   EnsemblBacteria; AAN42471; AAN42471; SF0838.
DR   EnsemblBacteria; AAP16343; AAP16343; S0878.
DR   GeneID; 1023829; -.
DR   GeneID; 58389704; -.
DR   KEGG; sfl:SF0838; -.
DR   KEGG; sfx:S0878; -.
DR   PATRIC; fig|198214.7.peg.967; -.
DR   HOGENOM; CLU_018816_14_1_6; -.
DR   OMA; TGKIQPE; -.
DR   OrthoDB; 1532186at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0019898; C:extrinsic component of membrane; IEA:InterPro.
DR   GO; GO:1990195; C:macrolide transmembrane transporter complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR   GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IEA:InterPro.
DR   InterPro; IPR032317; HlyD_D23.
DR   InterPro; IPR030190; MacA.
DR   InterPro; IPR006143; RND_pump_MFP.
DR   PANTHER; PTHR30469:SF34; PTHR30469:SF34; 1.
DR   Pfam; PF16576; HlyD_D23; 1.
DR   TIGRFAMs; TIGR01730; RND_mfp; 1.
PE   3: Inferred from homology;
KW   Antibiotic resistance; Cell inner membrane; Cell membrane; Coiled coil;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..371
FT                   /note="Macrolide export protein MacA"
FT                   /id="PRO_0000018697"
FT   TOPO_DOM        1..10
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..371
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   COILED          92..137
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   371 AA;  40639 MW;  25F7D3CB1A2D080F CRC64;
     MKKRKTVKKR YVIALVIVIA GLITLWRILN APVPTYQTLI VRPGDLQQSV LATGKLDALR
     KVDVGAQVSG QLKTLSVAIG DKVKKDQLLG VIDPEQAENQ IKEVEATLME LRAQRQQAEA
     ELKLARVTYS RQQRLAQTQA VSLQDLDTAA TEMAVKQAQI GTIDAQIKRN QASLDTAKTN
     LDYTRIVAPM AGEVTQITTL QGQTVIAAQQ APNILTLADM STMLVKAQVS EADVIHLKPG
     QKAWFTVLGD PLTRYEGQIK DVLPTPEKVN DAIFYYARFE VPNPNGLLRL DMTAQVHIQL
     TDVKNVLTIP LSALGDPVGD NRYKVKLLRN GETREREVTI GARNDTDVEI VKGLEAGDEV
     VIGEAKPGAA Q