AMIC_ECOLI
ID AMIC_ECOLI Reviewed; 417 AA.
AC P63883; Q2MA20; Q46929;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase AmiC;
DE EC=3.5.1.28;
DE Flags: Precursor;
GN Name=amiC; Synonyms=ygdN; OrderedLocusNames=b2817, JW5449;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP FUNCTION AS AN AMIDASE, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC1061 / ATCC 53338 / DSM 7140;
RX PubMed=11454209; DOI=10.1046/j.1365-2958.2001.02499.x;
RA Heidrich C., Templin M.F., Ursinus A., Merdanovic M., Berger J.,
RA Schwarz H., de Pedro M.A., Holtje J.V.;
RT "Involvement of N-acetylmuramyl-L-alanine amidases in cell separation and
RT antibiotic-induced autolysis of Escherichia coli.";
RL Mol. Microbiol. 41:167-178(2001).
RN [4]
RP EXPORT VIA THE TAT-SYSTEM AND THE SEC-SYSTEM.
RX PubMed=17218314; DOI=10.1074/jbc.m610507200;
RA Tullman-Ercek D., DeLisa M.P., Kawarasaki Y., Iranpour P., Ribnicky B.,
RA Palmer T., Georgiou G.;
RT "Export pathway selectivity of Escherichia coli twin arginine translocation
RT signal peptides.";
RL J. Biol. Chem. 282:8309-8316(2007).
RN [5]
RP SUBCELLULAR LOCATION, EXPORT VIA THE TAT-SYSTEM, AND DOMAIN.
RC STRAIN=K12;
RX PubMed=12787347; DOI=10.1046/j.1365-2958.2003.03511.x;
RA Bernhardt T.G., de Boer P.A.;
RT "The Escherichia coli amidase AmiC is a periplasmic septal ring component
RT exported via the twin-arginine transport pathway.";
RL Mol. Microbiol. 48:1171-1182(2003).
RN [6]
RP FUNCTION.
RC STRAIN=K12;
RX PubMed=18390656; DOI=10.1128/jb.00207-08;
RA Uehara T., Park J.T.;
RT "Growth of Escherichia coli: significance of peptidoglycan degradation
RT during elongation and septation.";
RL J. Bacteriol. 190:3914-3922(2008).
CC -!- FUNCTION: Cell-wall hydrolase involved in septum cleavage during cell
CC division. Can also act as powerful autolysin in the presence of murein
CC synthesis inhibitors. {ECO:0000269|PubMed:11454209,
CC ECO:0000269|PubMed:18390656}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:12787347}.
CC Note=Present throughout the periplasm in non-dividing cells, but
CC localizes almost exclusively to a ring at the site of constriction in
CC dividing cells.
CC -!- DOMAIN: N-terminal domain is required and sufficient for targeting to
CC the septal ring. {ECO:0000269|PubMed:12787347}.
CC -!- PTM: Exported by the Tat system. The position of the signal peptide
CC cleavage has not been experimentally proven. Can also be exported by
CC the Sec system.
CC -!- DISRUPTION PHENOTYPE: Mutants are growing in chains of 3 to 6 cells.
CC {ECO:0000269|PubMed:11454209}.
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40464.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U29581; AAB40464.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75856.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE76886.1; -; Genomic_DNA.
DR RefSeq; NP_417294.4; NC_000913.3.
DR RefSeq; WP_000016907.1; NZ_STEB01000034.1.
DR PDB; 4BIN; X-ray; 2.49 A; A=35-417.
DR PDBsum; 4BIN; -.
DR AlphaFoldDB; P63883; -.
DR SMR; P63883; -.
DR BioGRID; 4261169; 248.
DR IntAct; P63883; 2.
DR STRING; 511145.b2817; -.
DR jPOST; P63883; -.
DR PaxDb; P63883; -.
DR PRIDE; P63883; -.
DR EnsemblBacteria; AAC75856; AAC75856; b2817.
DR EnsemblBacteria; BAE76886; BAE76886; BAE76886.
DR GeneID; 66673316; -.
DR GeneID; 947293; -.
DR KEGG; ecj:JW5449; -.
DR KEGG; eco:b2817; -.
DR PATRIC; fig|1411691.4.peg.3919; -.
DR EchoBASE; EB2895; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_2_2_6; -.
DR InParanoid; P63883; -.
DR OMA; KRYFAAN; -.
DR PhylomeDB; P63883; -.
DR BioCyc; EcoCyc:G7458-MON; -.
DR BioCyc; MetaCyc:G7458-MON; -.
DR PRO; PR:P63883; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0042597; C:periplasmic space; IDA:EcoliWiki.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IDA:EcoCyc.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IDA:EcoCyc.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd02696; MurNAc-LAA; 1.
DR InterPro; IPR021731; AMIN_dom.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF11741; AMIN; 1.
DR SMART; SM00646; Ami_3; 1.
DR PROSITE; PS51318; TAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell wall biogenesis/degradation; Hydrolase; Periplasm;
KW Reference proteome; Signal.
FT SIGNAL 1..31
FT /note="Tat-type signal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT CHAIN 32..417
FT /note="N-acetylmuramoyl-L-alanine amidase AmiC"
FT /id="PRO_0000006465"
FT DOMAIN 190..404
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000255"
FT REGION 166..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 35..42
FT /evidence="ECO:0007829|PDB:4BIN"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:4BIN"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:4BIN"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:4BIN"
FT STRAND 70..77
FT /evidence="ECO:0007829|PDB:4BIN"
FT HELIX 82..85
FT /evidence="ECO:0007829|PDB:4BIN"
FT HELIX 86..90
FT /evidence="ECO:0007829|PDB:4BIN"
FT STRAND 96..107
FT /evidence="ECO:0007829|PDB:4BIN"
FT STRAND 110..119
FT /evidence="ECO:0007829|PDB:4BIN"
FT STRAND 121..128
FT /evidence="ECO:0007829|PDB:4BIN"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:4BIN"
FT HELIX 155..159
FT /evidence="ECO:0007829|PDB:4BIN"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:4BIN"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:4BIN"
FT HELIX 211..226
FT /evidence="ECO:0007829|PDB:4BIN"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:4BIN"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:4BIN"
FT HELIX 246..255
FT /evidence="ECO:0007829|PDB:4BIN"
FT STRAND 259..265
FT /evidence="ECO:0007829|PDB:4BIN"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:4BIN"
FT STRAND 276..282
FT /evidence="ECO:0007829|PDB:4BIN"
FT HELIX 290..300
FT /evidence="ECO:0007829|PDB:4BIN"
FT HELIX 302..306
FT /evidence="ECO:0007829|PDB:4BIN"
FT HELIX 324..343
FT /evidence="ECO:0007829|PDB:4BIN"
FT TURN 344..346
FT /evidence="ECO:0007829|PDB:4BIN"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:4BIN"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:4BIN"
FT HELIX 360..362
FT /evidence="ECO:0007829|PDB:4BIN"
FT STRAND 369..373
FT /evidence="ECO:0007829|PDB:4BIN"
FT HELIX 380..386
FT /evidence="ECO:0007829|PDB:4BIN"
FT HELIX 389..406
FT /evidence="ECO:0007829|PDB:4BIN"
SQ SEQUENCE 417 AA; 45634 MW; 76F8F733DCCC36D7 CRC64;
MSGSNTAISR RRLLQGAGAM WLLSVSQVSL AAVSQVVAVR VWPASSYTRV TVESNRQLKY
KQFALSNPER VVVDIEDVNL NSVLKGMAAQ IRADDPFIKS ARVGQFDPQT VRMVFELKQN
VKPQLFALAP VAGFKERLVM DLYPANAQDM QDPLLALLED YNKGDLEKQV PPAQSGPQPG
KAGRDRPIVI MLDPGHGGED SGAVGKYKTR EKDVVLQIAR RLRSLIEKEG NMKVYMTRNE
DIFIPLQVRV AKAQKQRADL FVSIHADAFT SRQPSGSSVF ALSTKGATST AAKYLAQTQN
ASDLIGGVSK SGDRYVDHTM FDMVQSLTIA DSLKFGKAVL NKLGKINKLH KNQVEQAGFA
VLKAPDIPSI LVETAFISNV EEERKLKTAT FQQEVAESIL AGIKAYFADG ATLARRG
