AMPG_ECOLI
ID AMPG_ECOLI Reviewed; 491 AA.
AC P0AE16; P36670; Q2MBZ3;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Anhydromuropeptide permease {ECO:0000303|PubMed:15728916};
DE AltName: Full=AmpG permease {ECO:0000303|PubMed:12426329, ECO:0000303|PubMed:15728916};
DE AltName: Full=Muropeptide:H(+) symporter {ECO:0000305};
GN Name=ampG {ECO:0000303|PubMed:8231804}; OrderedLocusNames=b0433, JW0423;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8231804; DOI=10.1111/j.1365-2958.1993.tb01731.x;
RA Lindquist S., Weston-Hafer K., Schmidt H., Pul C., Korfmann G.,
RA Erickson J., Sanders C., Martin H.H., Normark S.;
RT "AmpG, a signal transducer in chromosomal beta-lactamase induction.";
RL Mol. Microbiol. 9:703-715(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=SN0301-1, SN0301-3, and SN0301-5;
RX PubMed=7773404; DOI=10.1099/13500872-141-5-1085;
RA Schmidt H., Korfmann G., Barth H., Martin H.H.;
RT "The signal transducer encoded by ampG is essential for induction of
RT chromosomal AmpC beta-lactamase in Escherichia coli by beta-lactam
RT antibiotics and 'unspecific' inducers.";
RL Microbiology 141:1085-1092(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
RP FUNCTION AS A PERMEASE.
RX PubMed=8878601; DOI=10.1128/aac.40.9.2173;
RA Dietz H., Pfeifle D., Wiedemann B.;
RT "Location of N-acetylmuramyl-L-alanyl-D-glutamylmesodiaminopimelic acid,
RT presumed signal molecule for beta-lactamase induction, in the bacterial
RT cell.";
RL Antimicrob. Agents Chemother. 40:2173-2177(1996).
RN [7]
RP FUNCTION, AND ACTIVITY REGULATION.
RC STRAIN=K12;
RX PubMed=12426329; DOI=10.1128/jb.184.23.6434-6436.2002;
RA Cheng Q., Park J.T.;
RT "Substrate specificity of the AmpG permease required for recycling of cell
RT wall anhydro-muropeptides.";
RL J. Bacteriol. 184:6434-6436(2002).
RN [8]
RP SUBCELLULAR LOCATION, TOPOLOGY, AND DOMAIN.
RX PubMed=15728916; DOI=10.1128/aac.49.3.1145-1149.2005;
RA Chahboune A., Decaffmeyer M., Brasseur R., Joris B.;
RT "Membrane topology of the Escherichia coli AmpG permease required for
RT recycling of cell wall anhydromuropeptides and AmpC beta-lactamase
RT induction.";
RL Antimicrob. Agents Chemother. 49:1145-1149(2005).
RN [9]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Permease involved in cell wall peptidoglycan recycling
CC (PubMed:8878601, PubMed:12426329). Transports, from the periplasm into
CC the cytoplasm, the disaccharide N-acetylglucosaminyl-beta-1,4-anhydro-
CC N-acetylmuramic acid (GlcNAc-anhMurNAc) and GlcNAc-anhMurNAc-peptides
CC (PubMed:12426329). Transport is dependent on the proton motive force
CC (PubMed:12426329). AmpG is also involved in beta-lactamase induction
CC (PubMed:7773404). {ECO:0000269|PubMed:12426329,
CC ECO:0000269|PubMed:7773404, ECO:0000269|PubMed:8878601}.
CC -!- ACTIVITY REGULATION: Uptake is inhibited by carbonyl cyanide m-
CC chlorophenylhydrazone (CCCP). {ECO:0000269|PubMed:12426329}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15728916,
CC ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15728916}.
CC -!- DOMAIN: Four hydrophobic segments are not embedded in the cytoplasmic
CC membrane and form two large cytoplasmic loops.
CC {ECO:0000269|PubMed:15728916}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily.
CC {ECO:0000305}.
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DR EMBL; S67816; AAB28884.1; -; Genomic_DNA.
DR EMBL; X82158; CAA57651.1; -; mRNA.
DR EMBL; X82159; CAA57652.1; -; mRNA.
DR EMBL; X82160; CAA57653.1; -; mRNA.
DR EMBL; U82664; AAB40189.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73536.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76213.1; -; Genomic_DNA.
DR PIR; S37391; S37391.
DR RefSeq; NP_414967.1; NC_000913.3.
DR RefSeq; WP_000098429.1; NZ_SSZK01000009.1.
DR AlphaFoldDB; P0AE16; -.
DR SMR; P0AE16; -.
DR BioGRID; 4259838; 195.
DR STRING; 511145.b0433; -.
DR TCDB; 2.A.1.25.2; the major facilitator superfamily (mfs).
DR PaxDb; P0AE16; -.
DR PRIDE; P0AE16; -.
DR EnsemblBacteria; AAC73536; AAC73536; b0433.
DR EnsemblBacteria; BAE76213; BAE76213; BAE76213.
DR GeneID; 946438; -.
DR KEGG; ecj:JW0423; -.
DR KEGG; eco:b0433; -.
DR PATRIC; fig|1411691.4.peg.1844; -.
DR EchoBASE; EB2100; -.
DR eggNOG; COG2223; Bacteria.
DR HOGENOM; CLU_029352_1_0_6; -.
DR InParanoid; P0AE16; -.
DR OMA; ANPFYVD; -.
DR PhylomeDB; P0AE16; -.
DR BioCyc; EcoCyc:AMPG-MON; -.
DR BioCyc; MetaCyc:AMPG-MON; -.
DR PRO; PR:P0AE16; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015295; F:solute:proton symporter activity; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0015835; P:peptidoglycan transport; IBA:GO_Central.
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 1: Evidence at protein level;
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_0000084830"
FT TOPO_DOM 1..11
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15728916"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:15728916"
FT TOPO_DOM 33..47
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15728916"
FT TRANSMEM 48..61
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:15728916"
FT TOPO_DOM 62..81
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15728916"
FT TRANSMEM 82..105
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:15728916"
FT TOPO_DOM 106
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15728916"
FT TRANSMEM 107..124
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:15728916"
FT TOPO_DOM 125..221
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15728916"
FT TRANSMEM 222..240
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:15728916"
FT TOPO_DOM 241..264
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15728916"
FT TRANSMEM 265..284
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:15728916"
FT TOPO_DOM 285..287
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15728916"
FT TRANSMEM 288..303
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:15728916"
FT TOPO_DOM 304..327
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15728916"
FT TRANSMEM 328..346
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:15728916"
FT TOPO_DOM 347..421
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15728916"
FT TRANSMEM 422..453
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:15728916"
FT TOPO_DOM 454..457
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:15728916"
FT TRANSMEM 458..485
FT /note="Helical"
FT /evidence="ECO:0000305|PubMed:15728916"
FT TOPO_DOM 486..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15728916,
FT ECO:0000269|PubMed:15919996"
FT VARIANT 151
FT /note="G -> D (in non-inducible mutant SN0301-1)"
FT VARIANT 268
FT /note="G -> D (in non-inducible mutant SN0301-3)"
FT VARIANT 373
FT /note="G -> D (in non-inducible mutant SN0301-5)"
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
