ID G5ZY05_9PROT Unreviewed; 430 AA.
AC G5ZY05;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=HIMB100_00009060 {ECO:0000313|EMBL:EHI49336.1};
OS SAR116 cluster alpha proteobacterium HIMB100.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; SAR116 cluster.
OX NCBI_TaxID=909943 {ECO:0000313|EMBL:EHI49336.1, ECO:0000313|Proteomes:UP000004261};
RN [1] {ECO:0000313|EMBL:EHI49336.1, ECO:0000313|Proteomes:UP000004261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain HIMB100 {ECO:0000313|Proteomes:UP000004261};
RX PubMed=22675578; DOI=10.4056/sigs.1854551;
RA Grote J., Bayindirli C., Bergauer K., Carpintero de Moraes P., Chen H.,
RA D'Ambrosio L., Edwards B., Fernandez-Gomez B., Hamisi M., Logares R.,
RA Nguyen D., Rii Y.M., Saeck E., Schutte C., Widner B., Church M.J.,
RA Steward G.F., Karl D.M., Delong E.F., Eppley J.M., Schuster S.C.,
RA Kyrpides N.C., Rappe M.S.;
RT "Draft genome sequence of strain HIMB100, a cultured representative of the
RT SAR116 clade of marine Alphaproteobacteria.";
RL Stand. Genomic Sci. 5:269-278(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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHI49336.1}.
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DR EMBL; AFXB01000006; EHI49336.1; -; Genomic_DNA.
DR AlphaFoldDB; G5ZY05; -.
DR STRING; 909943.HIMB100_00009060; -.
DR PATRIC; fig|909943.3.peg.922; -.
DR eggNOG; COG0860; Bacteria.
DR Proteomes; UP000004261; Unassembled WGS sequence.
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; 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 SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000004261}.
FT DOMAIN 268..422
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 162..197
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 179..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 430 AA; 46211 MW; FF86B179B9F67C39 CRC64;
MIDGLGRKLV FLFLFMLGAL DVGQTAIAAD NQLTGMRLGM IDLNGAPALR IVIETRQPAS
AKLLLLDEPW RVVIDSPGLT WDIAALQSAG TLSNGPATAY RFGHPQPGTG RLVIEMDEPA
SPERAFTLPP RDAGGYRLVI DLVDKGPTRF KLAQRSLKKD GYAVTSAGHK PPVDSSAEQA
DIRQPTSQQV SVASPAPRPA QLNRKWIIAI DAGHGGKDPG ALGRGGTKEK DITLAAAKQL
AADLNATGKV SARLTRSSDK FLKLRQRIAI AREMSADVFI SLHADSALRK SARGMSVFTL
SDTASDKEAA YIARRENKAD LVGGPDLAVE DPAAANALLS MFQRETMNES SRLAAAILKQ
IKDMPGGDKR GHRFAGFAVL KSPDVPSVLV EMGFLSNAED ENNLNSERYR RKLTQRLAKA
IVTYLTTPLS
//
