ID C5WCI4_9ENTR Unreviewed; 483 AA.
AC C5WCI4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN Name=amiB {ECO:0000313|EMBL:BAH83040.1};
GN ORFNames=ICMP_179 {ECO:0000313|EMBL:BAH83040.1};
OS Candidatus Ishikawaella capsulata Mpkobe.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Ishikawaella.
OX NCBI_TaxID=476281 {ECO:0000313|EMBL:BAH83040.1, ECO:0000313|Proteomes:UP000061704};
RN [1] {ECO:0000313|EMBL:BAH83040.1, ECO:0000313|Proteomes:UP000061704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mpkobe {ECO:0000313|EMBL:BAH83040.1,
RC ECO:0000313|Proteomes:UP000061704};
RX PubMed=21737395;
RA Nikoh N., Hosokawa T., Ohshima K., Hattori M., Fukatsu T.;
RT "Reductive evolution of bacterial genome in insect gut environment.";
RL Genome Biol. Evol. 3:702-714(2011).
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; AP010872; BAH83040.1; -; Genomic_DNA.
DR RefSeq; WP_041068906.1; NZ_AP010872.1.
DR AlphaFoldDB; C5WCI4; -.
DR STRING; 476281.ICMP_179; -.
DR KEGG; icp:ICMP_179; -.
DR HOGENOM; CLU_014322_2_3_6; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000061704; 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; 1.
DR CDD; cd02696; MurNAc-LAA; 1.
DR Gene3D; 3.10.350.10; LysM domain; 1.
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; 1.
DR SMART; SM00646; Ami_3; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000061704};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..483
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002956120"
FT DOMAIN 435..478
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 483 AA; 55414 MW; D3B696340E96C1B4 CRC64;
MILRISYKYI GLIYLLTGLT CAADPCHIQV VNTSTDARII LRFNKNPDYT YVFRNYNKEL
ILNINNIDVS KIFELNFNKD NYIKSIQYFN DDSDHYKNKL IFEFPYNTKV TVSKKITNSK
KNIILNVAKT MPDPIYDDDQ TSYDDLLKKN NFLCKTNIDK KITIALDPGH GGGDPGAIGQ
NGLYEKTINF KIACKLQKLL NNNPMFDCFL IRDKDERVHL DQRKDIARQR HANILISIHA
NSIHNPLIHG ASTWILSHDR FITEINNWVG SHPQNLQSLA EIGPVFNCKM DDILRKVILD
VEYHYWNHIS MAVSIKILKK LKDLYKITYF KEMKILDNVL KLDKKTTQRA GFSVLCSPDI
PSVIIETGFL SYTSEASLLS TDAYQNQLAE SIYHGMVNYF CKNSYPEIST TTKLLSLHTN
NASINHNKEY VVEDMKYLVK EGDTLYSISK KYGVSTPLLS DLNHLNSNTI SVGNFLTITS
NKK
//
