MACB_ECOLI
ID MACB_ECOLI Reviewed; 648 AA.
AC P75831;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 177.
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}; Synonyms=ybjZ;
GN OrderedLocusNames=b0879, JW0863;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN MACROLIDE TRANSPORT, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / W3104 / ATCC 19020;
RX PubMed=11544226; DOI=10.1128/jb.183.19.5639-5644.2001;
RA Kobayashi N., Nishino K., Yamaguchi A.;
RT "Novel macrolide-specific ABC-type efflux transporter in Escherichia
RT coli.";
RL J. Bacteriol. 183:5639-5644(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP TOPOLOGY.
RC STRAIN=K12 / W3104 / ATCC 19020;
RX PubMed=12832048; DOI=10.1016/s0014-5793(03)00579-9;
RA Kobayashi N., Nishino K., Hirata T., Yamaguchi A.;
RT "Membrane topology of ABC-type macrolide antibiotic exporter MacB in
RT Escherichia coli.";
RL FEBS Lett. 546:241-246(2003).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP INTERACTION WITH MACA, SUBCELLULAR LOCATION, AND MUTAGENESIS OF LYS-47 AND
RP ASP-169.
RC STRAIN=K12;
RX PubMed=17214741; DOI=10.1111/j.1365-2958.2006.05549.x;
RA Tikhonova E.B., Devroy V.K., Lau S.Y., Zgurskaya H.I.;
RT "Reconstitution of the Escherichia coli macrolide transporter: the
RT periplasmic membrane fusion protein MacA stimulates the ATPase activity of
RT MacB.";
RL Mol. Microbiol. 63:895-910(2007).
RN [7]
RP FUNCTION, ACTIVITY REGULATION, SUBUNIT, AND INTERACTION WITH MACA.
RX PubMed=18955484; DOI=10.1074/jbc.m806964200;
RA Lin H.T., Bavro V.N., Barrera N.P., Frankish H.M., Velamakanni S.,
RA van Veen H.W., Robinson C.V., Borges-Walmsley M.I., Walmsley A.R.;
RT "MacB ABC transporter is a dimer whose ATPase activity and macrolide-
RT binding capacity are regulated by the membrane fusion protein MacA.";
RL J. Biol. Chem. 284:1145-1154(2009).
RN [8]
RP ACTIVITY REGULATION, AND INTERACTION WITH MACA.
RX PubMed=21696464; DOI=10.1111/j.1365-2958.2011.07744.x;
RA Modali S.D., Zgurskaya H.I.;
RT "The periplasmic membrane proximal domain of MacA acts as a switch in
RT stimulation of ATP hydrolysis by MacB transporter.";
RL Mol. Microbiol. 81:937-951(2011).
RN [9]
RP FUNCTION.
RX PubMed=23974027; DOI=10.1128/jb.00756-13;
RA Lu S., Zgurskaya H.I.;
RT "MacA, a periplasmic membrane fusion protein of the macrolide transporter
RT MacAB-TolC, binds lipopolysaccharide core specifically and with high
RT affinity.";
RL J. Bacteriol. 195:4865-4872(2013).
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. When
CC overexpressed, the system confers resistance against macrolides
CC composed of 14- and 15-membered lactones but no or weak resistance
CC against 16-membered ones. In addition, the system could also transport
CC R-LPS or a similar glycolipid. {ECO:0000269|PubMed:11544226,
CC ECO:0000269|PubMed:17214741, ECO:0000269|PubMed:18955484,
CC ECO:0000269|PubMed:23974027}.
CC -!- ACTIVITY REGULATION: ATPase activity is stimulated by interaction with
CC MacA and inhibited by vanadate. {ECO:0000269|PubMed:17214741,
CC ECO:0000269|PubMed:18955484, ECO:0000269|PubMed:21696464}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.38 mM for ATP (in the presence of MacA)
CC {ECO:0000269|PubMed:17214741};
CC KM=2.30 mM for ATP (in the absence of MacA)
CC {ECO:0000269|PubMed:17214741};
CC Note=kcat is 0.78 sec(-1) for ATP in the presence of MacA. kcat is
CC 0.10 sec(-1) for ATP in the absence of MacA.;
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, ECO:0000269|PubMed:17214741,
CC ECO:0000269|PubMed:18955484, ECO:0000269|PubMed:21696464}.
CC -!- INTERACTION:
CC P75831; P75830: macA; NbExp=3; IntAct=EBI-1125580, EBI-551961;
CC P75831; P75831: macB; NbExp=4; IntAct=EBI-1125580, EBI-1125580;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01720, ECO:0000269|PubMed:11544226,
CC ECO:0000269|PubMed:17214741}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01720, ECO:0000269|PubMed:11544226,
CC ECO:0000269|PubMed:17214741}.
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; AB071146; BAB64542.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73966.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35598.1; -; Genomic_DNA.
DR PIR; G64826; G64826.
DR RefSeq; NP_415400.1; NC_000913.3.
DR RefSeq; WP_000188144.1; NZ_SSZK01000002.1.
DR PDB; 5LJ8; X-ray; 1.95 A; A/B=309-508.
DR PDB; 5LJ9; X-ray; 2.30 A; A/B/C=1-223.
DR PDB; 5LJA; X-ray; 2.40 A; A=1-223.
DR PDB; 5NIK; EM; 3.30 A; J/K=1-648.
DR PDB; 5NIL; EM; 5.30 A; J/K=1-648.
DR PDBsum; 5LJ8; -.
DR PDBsum; 5LJ9; -.
DR PDBsum; 5LJA; -.
DR PDBsum; 5NIK; -.
DR PDBsum; 5NIL; -.
DR AlphaFoldDB; P75831; -.
DR SMR; P75831; -.
DR BioGRID; 4261698; 111.
DR ComplexPortal; CPX-2107; MacAB-TolC ABC transporter complex.
DR IntAct; P75831; 3.
DR STRING; 511145.b0879; -.
DR TCDB; 3.A.1.122.1; the atp-binding cassette (abc) superfamily.
DR jPOST; P75831; -.
DR PaxDb; P75831; -.
DR PRIDE; P75831; -.
DR EnsemblBacteria; AAC73966; AAC73966; b0879.
DR EnsemblBacteria; BAA35598; BAA35598; BAA35598.
DR GeneID; 945164; -.
DR KEGG; ecj:JW0863; -.
DR KEGG; eco:b0879; -.
DR PATRIC; fig|1411691.4.peg.1398; -.
DR EchoBASE; EB3459; -.
DR eggNOG; COG0577; Bacteria.
DR eggNOG; COG1136; Bacteria.
DR HOGENOM; CLU_000604_78_2_6; -.
DR InParanoid; P75831; -.
DR OMA; VVILITH; -.
DR PhylomeDB; P75831; -.
DR BioCyc; EcoCyc:MACB; -.
DR BioCyc; MetaCyc:MACB; -.
DR PRO; PR:P75831; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoliWiki.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:1990196; C:MacAB-TolC complex; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0008559; F:ABC-type xenobiotic transporter activity; IDA:EcoCyc.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0046677; P:response to antibiotic; IDA:EcoCyc.
DR GO; GO:1990961; P:xenobiotic detoxification by transmembrane export across the plasma membrane; IDA:ComplexPortal.
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; Reference proteome;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..648
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000092474"
FT TOPO_DOM 1..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 273..293
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TOPO_DOM 294..522
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 523..543
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TOPO_DOM 544..575
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 576..596
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TOPO_DOM 597..610
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 611..631
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01720"
FT TOPO_DOM 632..648
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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"
FT MUTAGEN 47
FT /note="K->L: Lack of activity."
FT /evidence="ECO:0000269|PubMed:17214741"
FT MUTAGEN 169
FT /note="D->N: Lack of activity."
FT /evidence="ECO:0000269|PubMed:17214741"
FT STRAND 4..16
FT /evidence="ECO:0007829|PDB:5LJ9"
FT STRAND 19..31
FT /evidence="ECO:0007829|PDB:5LJ9"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:5LJ9"
FT HELIX 47..54
FT /evidence="ECO:0007829|PDB:5LJ9"
FT STRAND 61..67
FT /evidence="ECO:0007829|PDB:5LJ9"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:5LJ9"
FT HELIX 77..87
FT /evidence="ECO:0007829|PDB:5LJ9"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:5LJ9"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:5NIK"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:5LJ9"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:5LJ9"
FT HELIX 118..131
FT /evidence="ECO:0007829|PDB:5LJ9"
FT HELIX 135..137
FT /evidence="ECO:0007829|PDB:5LJ9"
FT HELIX 142..144
FT /evidence="ECO:0007829|PDB:5LJ9"
FT HELIX 147..158
FT /evidence="ECO:0007829|PDB:5LJ9"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:5LJ9"
FT STRAND 164..170
FT /evidence="ECO:0007829|PDB:5LJ9"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:5LJ9"
FT HELIX 177..192
FT /evidence="ECO:0007829|PDB:5LJ9"
FT STRAND 196..202
FT /evidence="ECO:0007829|PDB:5LJ9"
FT HELIX 204..207
FT /evidence="ECO:0007829|PDB:5LJ9"
FT STRAND 210..217
FT /evidence="ECO:0007829|PDB:5LJ9"
FT STRAND 220..223
FT /evidence="ECO:0007829|PDB:5LJ9"
FT HELIX 248..267
FT /evidence="ECO:0007829|PDB:5NIK"
FT HELIX 269..305
FT /evidence="ECO:0007829|PDB:5NIK"
FT STRAND 311..319
FT /evidence="ECO:0007829|PDB:5LJ8"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:5LJ8"
FT HELIX 333..340
FT /evidence="ECO:0007829|PDB:5LJ8"
FT STRAND 345..360
FT /evidence="ECO:0007829|PDB:5LJ8"
FT STRAND 363..372
FT /evidence="ECO:0007829|PDB:5LJ8"
FT HELIX 376..380
FT /evidence="ECO:0007829|PDB:5LJ8"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:5LJ8"
FT HELIX 392..396
FT /evidence="ECO:0007829|PDB:5LJ8"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:5LJ8"
FT HELIX 406..412
FT /evidence="ECO:0007829|PDB:5LJ8"
FT STRAND 423..426
FT /evidence="ECO:0007829|PDB:5LJ8"
FT STRAND 429..438
FT /evidence="ECO:0007829|PDB:5LJ8"
FT HELIX 444..446
FT /evidence="ECO:0007829|PDB:5NIK"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:5LJ8"
FT HELIX 456..459
FT /evidence="ECO:0007829|PDB:5LJ8"
FT TURN 460..464
FT /evidence="ECO:0007829|PDB:5NIK"
FT STRAND 465..476
FT /evidence="ECO:0007829|PDB:5LJ8"
FT HELIX 482..497
FT /evidence="ECO:0007829|PDB:5LJ8"
FT STRAND 502..507
FT /evidence="ECO:0007829|PDB:5LJ8"
FT HELIX 508..550
FT /evidence="ECO:0007829|PDB:5NIK"
FT HELIX 552..560
FT /evidence="ECO:0007829|PDB:5NIK"
FT HELIX 565..600
FT /evidence="ECO:0007829|PDB:5NIK"
FT HELIX 611..638
FT /evidence="ECO:0007829|PDB:5NIK"
FT HELIX 641..646
FT /evidence="ECO:0007829|PDB:5NIK"
SQ SEQUENCE 648 AA; 70702 MW; 157B7D6E1ED17346 CRC64;
MTPLLELKDI RRSYPAGDEQ VEVLKGISLD IYAGEMVAIV GASGSGKSTL MNILGCLDKA
TSGTYRVAGQ DVATLDADAL AQLRREHFGF IFQRYHLLSH LTAEQNVEVP AVYAGLERKQ
RLLRAQELLQ RLGLEDRTEY YPAQLSGGQQ QRVSIARALM NGGQVILADE PTGALDSHSG
EEVMAILHQL RDRGHTVIIV THDPQVAAQA ERVIEIRDGE IVRNPPAIEK VNVTGGTEPV
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 STVTGILFGW LPARNAARLD PVDALARE
