ID   AMIB_ECOLI              Reviewed;         445 AA.
AC   P26365; Q2M6D6;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 2.
DT   03-AUG-2022, entry version 150.
DE   RecName: Full=N-acetylmuramoyl-L-alanine amidase AmiB;
DE            EC=3.5.1.28;
DE   Flags: Precursor;
GN   Name=amiB; Synonyms=yjeD; OrderedLocusNames=b4169, JW4127;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=7511774; DOI=10.1111/j.1365-2958.1994.tb00300.x;
RA   Tsui H.-C.T., Zhao G., Feng G., Leung H.-C.E., Winkler M.E.;
RT   "The mutL repair gene of Escherichia coli K-12 forms a superoperon with a
RT   gene encoding a new cell-wall amidase.";
RL   Mol. Microbiol. 11:189-202(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT   from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 362-445.
RC   STRAIN=K12;
RX   PubMed=1594459; DOI=10.1093/nar/20.9.2379;
RA   Tsui H.-C.T., Mandavilli B.S., Winkler M.E.;
RT   "Nonconserved segment of the MutL protein from Escherichia coli K-12 and
RT   Salmonella typhimurium.";
RL   Nucleic Acids Res. 20:2379-2379(1992).
RN   [6]
RP   FUNCTION AS AN AMIDASE.
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   [7]
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:0000250}.
CC   -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC       {ECO:0000305}.
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DR   EMBL; L19346; AAA20097.1; -; Unassigned_DNA.
DR   EMBL; U14003; AAA97065.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC77126.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78170.1; -; Genomic_DNA.
DR   EMBL; Z11831; CAA77851.1; -; Genomic_DNA.
DR   PIR; S41741; S41741.
DR   RefSeq; NP_418590.1; NC_000913.3.
DR   RefSeq; WP_000990333.1; NZ_STEB01000013.1.
DR   AlphaFoldDB; P26365; -.
DR   SMR; P26365; -.
DR   BioGRID; 4263189; 252.
DR   STRING; 511145.b4169; -.
DR   jPOST; P26365; -.
DR   PaxDb; P26365; -.
DR   PRIDE; P26365; -.
DR   EnsemblBacteria; AAC77126; AAC77126; b4169.
DR   EnsemblBacteria; BAE78170; BAE78170; BAE78170.
DR   GeneID; 948683; -.
DR   KEGG; ecj:JW4127; -.
DR   KEGG; eco:b4169; -.
DR   PATRIC; fig|1411691.4.peg.2532; -.
DR   EchoBASE; EB1338; -.
DR   eggNOG; COG0860; Bacteria.
DR   HOGENOM; CLU_014322_2_3_6; -.
DR   InParanoid; P26365; -.
DR   OMA; NADPMFK; -.
DR   PhylomeDB; P26365; -.
DR   BioCyc; EcoCyc:NACMURLALAAMI2-MON; -.
DR   BioCyc; MetaCyc:NACMURLALAAMI2-MON; -.
DR   PRO; PR:P26365; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
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; IPR002508; MurNAc-LAA_cat.
DR   Pfam; PF01520; Amidase_3; 1.
DR   SMART; SM00646; Ami_3; 1.
PE   1: Evidence at protein level;
KW   Cell wall biogenesis/degradation; Hydrolase; Periplasm; Reference proteome;
KW   Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..445
FT                   /note="N-acetylmuramoyl-L-alanine amidase AmiB"
FT                   /id="PRO_0000006462"
FT   DOMAIN          194..413
FT                   /note="MurNAc-LAA"
FT                   /evidence="ECO:0000255"
FT   REGION          424..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   445 AA;  47985 MW;  C79CC9FD77BFCD38 CRC64;
     MMYRIRNWLV ATLLLLCTPV GAATLSDIQV SNGNQQARIT LSFIGDPDYA FSHQSKRTVA
     LDIKQTGVIQ GLPLLFSGNN LVKAIRSGTP KDAQTLRLVV DLTENGKTEA VKRQNGSNYT
     VVFTINADVP PPPPPPPVVA KRVETPAVVA PRVSEPARNP FKTESNRTTG VISSNTVTRP
     AARATANTGD KIIIAIDAGH GGQDPGAIGP GGTREKNVTI AIARKLRTLL NDDPMFKGVL
     TRDGDYFISV MGRSDVARKQ NANFLVSIHA DAAPNRSATG ASVWVLSNRR ANSEMASWLE
     QHEKQSELLG GAGDVLANSQ SDPYLSQAVL DLQFGHSQRV GYDVATSMIS QLQRIGEIHK
     RRPEHASLGV LRSPDIPSVL VETGFISNNS EERLLASDDY QQQLAEAIYK GLRNYFLAHP
     MQSAPQGATA QTASTVTTPD RTLPN