ID Q65SD8_MANSM Unreviewed; 614 AA.
AC Q65SD8;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN Name=amiC {ECO:0000313|EMBL:AAU38122.1};
GN OrderedLocusNames=MS1515 {ECO:0000313|EMBL:AAU38122.1};
OS Mannheimia succiniciproducens (strain MBEL55E).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Basfia.
OX NCBI_TaxID=221988 {ECO:0000313|EMBL:AAU38122.1, ECO:0000313|Proteomes:UP000000607};
RN [1] {ECO:0000313|EMBL:AAU38122.1, ECO:0000313|Proteomes:UP000000607}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBEL55E {ECO:0000313|EMBL:AAU38122.1,
RC ECO:0000313|Proteomes:UP000000607};
RX PubMed=15378067; DOI=10.1038/nbt1010;
RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA Jeong H., Hur C.G., Kim J.J.;
RT "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT succiniciproducens.";
RL Nat. Biotechnol. 22:1275-1281(2004).
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 Evidence={ECO:0000256|ARBA:ARBA00001561};
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 3 family.
CC {ECO:0000256|ARBA:ARBA00010860}.
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DR EMBL; AE016827; AAU38122.1; -; Genomic_DNA.
DR AlphaFoldDB; Q65SD8; -.
DR STRING; 221988.MS1515; -.
DR KEGG; msu:MS1515; -.
DR eggNOG; COG0860; Bacteria.
DR eggNOG; COG1388; Bacteria.
DR HOGENOM; CLU_014322_2_4_6; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000000607; Chromosome.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:UniProtKB-EC.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd00118; LysM; 4.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 3.10.350.10; LysM domain; 4.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR PANTHER; PTHR30404:SF6; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIB; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF01476; LysM; 4.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00257; LysM; 4.
DR SUPFAM; SSF54106; LysM domain; 4.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51782; LYSM; 4.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..614
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004269078"
FT DOMAIN 296..339
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 368..411
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 447..490
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 526..569
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 416..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 577..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..439
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..604
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 614 AA; 68197 MW; E3A39A65BDA88668 CRC64;
MKRFFLLFLT ALFFAINPAW AAVWTIAIDP GHGGKDPGAI SRNLGIYEKN VTLSIAQELK
GILDRDPNFR AVLTRRADYY ISVPQRSEIA RKNKANYLVS IHADSSENPA LKGASVWVLS
NRRANDEMGQ WLEDHEKQSE LLGGAGSVLS NHGSEKYLNQ TVLDLQFGHS QRTGYELGRS
ILRNFAKIAD LSRTSPQHAS LGVLRSPDIP SVLVETGYLS NATEEAKLSS PSYRKRIAYI
IYQGIVDFRK RHLGGEINTS SKIAGQMPTE KTQSANTAKA KDNFKDDKET VQDSGVRHKV
KSGETIAKIA GKYNVTSEEI ITLNKLKRKD LYIDELVKIP AEKTQSAKTA KAKDNFKDDN
ETVQDSGVRH KVKSGETIAK LARKYDVKSE DIVTLNKFKR KDLYIDELVK IPASAKNRQK
NEPVTNTKNT EKAENSAKTA KSELVNGSYT VKNGDTLFSI ANRFGVKQED IIELNKLKNA
NIFVGKKLKI PTGAKLKEDT KQQTKTNKTT KKETQAEPKT IEKATVSYTV KSGDSISRLA
NKFDVKAAEI IELNNLKNKE LHIGDKIKLP ANAKNVVTES KKTSVNKNTA VKGTKSSTKN
TTNKKTAKQD TKKK
//
