ID H8GKG1_METAL Unreviewed; 422 AA.
AC H8GKG1;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=Metal_2754 {ECO:0000313|EMBL:EIC30452.1};
OS Methylomicrobium album BG8.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomicrobium.
OX NCBI_TaxID=686340 {ECO:0000313|EMBL:EIC30452.1, ECO:0000313|Proteomes:UP000005090};
RN [1] {ECO:0000313|EMBL:EIC30452.1, ECO:0000313|Proteomes:UP000005090}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BG8 {ECO:0000313|EMBL:EIC30452.1,
RC ECO:0000313|Proteomes:UP000005090};
RX PubMed=23580712;
RA Kits K.D., Kalyuzhnaya M.G., Klotz M.G., Jetten M.S., Op den Camp H.J.,
RA Vuilleumier S., Bringel F., Dispirito A.A., Murrell J.C., Bruce D.,
RA Cheng J.F., Copeland A., Goodwin L., Hauser L., Lajus A., Land M.L.,
RA Lapidus A., Lucas S., Medigue C., Pitluck S., Woyke T., Zeytun A.,
RA Stein L.Y.;
RT "Genome Sequence of the Obligate Gammaproteobacterial Methanotroph
RT Methylomicrobium album Strain BG8.";
RL Genome Announc. 1:E0017013-E0017013(2013).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CM001475; EIC30452.1; -; Genomic_DNA.
DR RefSeq; WP_005373074.1; NZ_CM001475.1.
DR AlphaFoldDB; H8GKG1; -.
DR STRING; 686340.Metal_2754; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_2_3_6; -.
DR Proteomes; UP000005090; 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; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.60.40.3500; -; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR021731; AMIN_dom.
DR InterPro; IPR002508; MurNAc-LAA_cat.
DR PANTHER; PTHR30404; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; 1.
DR PANTHER; PTHR30404:SF0; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMIC; 1.
DR Pfam; PF01520; Amidase_3; 1.
DR Pfam; PF11741; AMIN; 1.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000005090};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..422
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003612276"
FT DOMAIN 251..406
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 131..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 422 AA; 45789 MW; 66B8B28E3E3F50A1 CRC64;
MRHFAKSFFL LALQLFSSVA FAAQVSVNSL HFWSSAKQSR MMIDVSAIPS HSISLTEHPG
RLVIDIQNAR LKGELSQPPA SHPFFSRIRT DQKQKTLRIV ADLKRQIDYE SFTLNPNKMY
GHRLVVDLTD KGPLSDSPNA SEKFSAQAAK PKAKAQAPQK LAKRAAGNDN PAKSAKGAAT
SAGPIGRNIV VAIDAGHGGE DPGAHGPAGT EEKRVVLAIA KKLAALINRQ RGMRAVLVRK
GDYYVDLRKR MEIARAANAD LFVSVHADAY QKSDVKGASV FTLSNRGASS EAARWLADSE
NAADLVGGVR LDDKEEVLAS VLLDLSQTAT LEASNNVAGQ VLKSFQNIGE LHFSSVQKAG
FLVLKSPDIP SILVETAFIS NPGEERKLNN TEHQSKIALA IFNGIRNYFK QYTPNDTRVA
EL
//
