AMPG_ECO57
ID AMPG_ECO57 Reviewed; 491 AA.
AC P0AE17; P36670;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Anhydromuropeptide permease {ECO:0000250|UniProtKB:P0AE16};
DE AltName: Full=AmpG permease {ECO:0000250|UniProtKB:P0AE16};
DE AltName: Full=Muropeptide:H(+) symporter {ECO:0000250|UniProtKB:P0AE16};
GN Name=ampG; OrderedLocusNames=Z0536, ECs0487;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Permease involved in cell wall peptidoglycan recycling.
CC Transports, from the periplasm into the cytoplasm, the disaccharide N-
CC acetylglucosaminyl-beta-1,4-anhydro-N-acetylmuramic acid (GlcNAc-
CC anhMurNAc) and GlcNAc-anhMurNAc-peptides. Transport is dependent on the
CC proton motive force. {ECO:0000250|UniProtKB:P0AE16}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0AE16}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P0AE16}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; AE005174; AAG54783.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB33910.1; -; Genomic_DNA.
DR PIR; C85540; C85540.
DR PIR; G90689; G90689.
DR RefSeq; NP_308514.1; NC_002695.1.
DR RefSeq; WP_000098429.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AE17; -.
DR SMR; P0AE17; -.
DR STRING; 155864.EDL933_0503; -.
DR EnsemblBacteria; AAG54783; AAG54783; Z0536.
DR EnsemblBacteria; BAB33910; BAB33910; ECs_0487.
DR GeneID; 914589; -.
DR KEGG; ece:Z0536; -.
DR KEGG; ecs:ECs_0487; -.
DR PATRIC; fig|386585.9.peg.588; -.
DR eggNOG; COG2223; Bacteria.
DR HOGENOM; CLU_029352_1_0_6; -.
DR OMA; ANPFYVD; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR004752; AmpG_permease/AT-1.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR PANTHER; PTHR12778; PTHR12778; 1.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cell wall biogenesis/degradation;
KW Membrane; Reference proteome; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..491
FT /note="Anhydromuropeptide permease"
FT /id="PRO_0000084831"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AE16"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AE16"
FT TOPO_DOM 33..47
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AE16"
FT TRANSMEM 48..61
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AE16"
FT TOPO_DOM 62..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AE16"
FT TRANSMEM 82..105
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AE16"
FT TOPO_DOM 106
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AE16"
FT TRANSMEM 107..124
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AE16"
FT TOPO_DOM 125..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AE16"
FT TRANSMEM 222..240
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AE16"
FT TOPO_DOM 241..264
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AE16"
FT TRANSMEM 265..284
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AE16"
FT TOPO_DOM 285..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AE16"
FT TRANSMEM 288..303
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AE16"
FT TOPO_DOM 304..327
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AE16"
FT TRANSMEM 328..346
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AE16"
FT TOPO_DOM 347..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AE16"
FT TRANSMEM 422..453
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AE16"
FT TOPO_DOM 454..457
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AE16"
FT TRANSMEM 458..485
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0AE16"
FT TOPO_DOM 486..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AE16"
SQ SEQUENCE 491 AA; 53245 MW; 6B0D7E2BC699CA9C CRC64;
MSSQYLRIFQ QPRSAILLIL GFASGLPLAL TSGTLQAWMT VENIDLKTIG FFSLVGQAYV
FKFLWSPLMD RYTPPFFGRR RGWLLATQIL LLVAIAAMGF LEPGTQLRWM AALAVVIAFC
SASQDIVFDA WKTDVLPAEE RGAGAAISVL GYRLGMLVSG GLALWLADKW LGWQGMYWLM
AALLIPCIIA TLLAPEPTDT IPVPKTLEQA VVAPLRDFFG RNNAWLILLL IVLYKLGDAF
AMSLTTTFLI RGVGFDAGEV GVVNKTLGLL ATIVGALYGG ILMQRLSLFR ALLIFGILQG
ASNAGYWLLS ITDKHLYSMG AAVFFENLCG GMGTSAFVAL LMTLCNKSFS ATQFALLSAL
SAVGRVYVGP VAGWFVEAHG WSTFYLFSVA AAVPGLILLL VCRQTLEYTR VNDNFISRTA
YPAGYAFAMW TLAAGVSLLA VWLLLLTMDA LDLTHFSFLP ALLEVGVLVA LSGVVLGGLL
DYLALRKTHL T
