MACB_ECOL5
ID MACB_ECOL5 Reviewed; 648 AA.
AC Q0TJH0;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
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=ECP_0894;
OS Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=362663;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=536 / UPEC;
RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT "Role of pathogenicity island-associated integrases in the genome
RT plasticity of uropathogenic Escherichia coli strain 536.";
RL Mol. Microbiol. 61:584-595(2006).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000247; ABG68909.1; -; Genomic_DNA.
DR RefSeq; WP_000188148.1; NC_008253.1.
DR PDB; 5C59; X-ray; 3.00 A; A/B/C/D/E/F/G=297-522.
DR PDBsum; 5C59; -.
DR AlphaFoldDB; Q0TJH0; -.
DR SMR; Q0TJH0; -.
DR STRING; 362663.ECP_0894; -.
DR EnsemblBacteria; ABG68909; ABG68909; ECP_0894.
DR KEGG; ecp:ECP_0894; -.
DR HOGENOM; CLU_000604_78_2_6; -.
DR OMA; VVILITH; -.
DR Proteomes; UP000009182; 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 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; ATP-binding; Cell inner membrane;
KW Cell membrane; Membrane; Nucleotide-binding; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..648
FT /note="Macrolide export ATP-binding/permease protein MacB"
FT /id="PRO_0000269942"
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 611..631
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"
FT STRAND 311..319
FT /evidence="ECO:0007829|PDB:5C59"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:5C59"
FT HELIX 333..340
FT /evidence="ECO:0007829|PDB:5C59"
FT STRAND 345..360
FT /evidence="ECO:0007829|PDB:5C59"
FT STRAND 363..372
FT /evidence="ECO:0007829|PDB:5C59"
FT HELIX 376..379
FT /evidence="ECO:0007829|PDB:5C59"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:5C59"
FT HELIX 392..396
FT /evidence="ECO:0007829|PDB:5C59"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:5C59"
FT HELIX 406..412
FT /evidence="ECO:0007829|PDB:5C59"
FT STRAND 423..426
FT /evidence="ECO:0007829|PDB:5C59"
FT STRAND 429..436
FT /evidence="ECO:0007829|PDB:5C59"
FT STRAND 451..455
FT /evidence="ECO:0007829|PDB:5C59"
FT HELIX 456..459
FT /evidence="ECO:0007829|PDB:5C59"
FT STRAND 468..476
FT /evidence="ECO:0007829|PDB:5C59"
FT HELIX 482..497
FT /evidence="ECO:0007829|PDB:5C59"
FT STRAND 502..506
FT /evidence="ECO:0007829|PDB:5C59"
SQ SEQUENCE 648 AA; 70618 MW; D323BFA84E425059 CRC64;
MTPLLELKDI RRSYPAGDEQ VEVLKGISLD IYAGEMVAIV GASGSGKSTL MNILGCLDKA
TSGTYRVAGQ DVATLDADAL AQLRREHFGF IFQRYHLLSH LTAEQNVEVP AVYAGLERKQ
RLLRAQELLQ RLGLEDRTEY YPAQLSGGQQ QRVSIARALM NGGQVILADE PTGALDSHSG
EEVMAILHQL RDRGHTVIIV THDPQVAAQA ERVIEIRDGE IVRNPPAVEK VNATGGTEPV
VNTASGWRQF VSGFNEALTM AWRALAANKM RTLLTMLGII IGIASVVSIV VVGDAAKQMV
LADIRSIGTN TIDVYPGNDF 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
