ID Q1QNV2_NITHX Unreviewed; 289 AA.
AC Q1QNV2;
DT 16-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 81.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN OrderedLocusNames=Nham_1270 {ECO:0000313|EMBL:ABE62095.1};
OS Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Nitrobacter.
OX NCBI_TaxID=323097 {ECO:0000313|EMBL:ABE62095.1, ECO:0000313|Proteomes:UP000001953};
RN [1] {ECO:0000313|EMBL:ABE62095.1, ECO:0000313|Proteomes:UP000001953}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10229 / NCIMB 13809 / X14
RC {ECO:0000313|Proteomes:UP000001953};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L.,
RA O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T.,
RA Gentry M.E., Bruce D., Richardson P.;
RT "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
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 2 family.
CC {ECO:0000256|ARBA:ARBA00007553}.
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DR EMBL; CP000319; ABE62095.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1QNV2; -.
DR STRING; 323097.Nham_1270; -.
DR KEGG; nha:Nham_1270; -.
DR eggNOG; COG3023; Bacteria.
DR HOGENOM; CLU_049290_2_2_5; -.
DR OMA; DIKPTRV; -.
DR OrthoDB; 9794842at2; -.
DR Proteomes; UP000001953; Chromosome.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd06583; PGRP; 1.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR Gene3D; 1.10.101.10; PGBD-like superfamily/PGBD; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR InterPro; IPR002477; Peptidoglycan-bd-like.
DR InterPro; IPR036365; PGBD-like_sf.
DR InterPro; IPR036366; PGBDSf.
DR PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR PANTHER; PTHR30417:SF1; N-ACETYLMURAMOYL-L-ALANINE AMIDASE BLYA; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR Pfam; PF01471; PG_binding_1; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000001953}.
FT DOMAIN 40..177
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 289 AA; 31623 MW; EA06971B27796778 CRC64;
MFASASSDLK RRCPLPIPKA LAGMSTFVPD SSVVSDTVPS LNFGDRAKGR QPDMIVLHYT
GMPDVEGALA RLCTSGTDVS AHYVVLEDGR IVQCVQEAKR AWHAGVASWA GEEDINSCSI
GIEIVNRGHD WGYPDFPLRQ VAAVIALCRG IILRRDIPAH RVVGHSDVAP ARKKDPGEKF
PWHSLADSGV GHWVRPSPIV RGDVLKTGSE GDDVRALQQS LARYGYGIKA SGTFDTPTME
VVTAFQRHFR PERVDGVADQ STLNTLRTLH ESLPDPDRRR GITRDQLRA
//