ID A3V477_9RHOB Unreviewed; 386 AA.
AC A3V477;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=SKA53_02771 {ECO:0000313|EMBL:EAQ07284.1};
OS Yoonia vestfoldensis SKA53.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Yoonia.
OX NCBI_TaxID=314232 {ECO:0000313|EMBL:EAQ07284.1, ECO:0000313|Proteomes:UP000004507};
RN [1] {ECO:0000313|EMBL:EAQ07284.1, ECO:0000313|Proteomes:UP000004507}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SKA53 {ECO:0000313|EMBL:EAQ07284.1,
RC ECO:0000313|Proteomes:UP000004507};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (JAN-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 -!- 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:EAQ07284.1}.
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DR EMBL; AAMS01000003; EAQ07284.1; -; Genomic_DNA.
DR RefSeq; WP_007204514.1; NZ_CH672414.1.
DR AlphaFoldDB; A3V477; -.
DR STRING; 314232.SKA53_02771; -.
DR eggNOG; COG0860; Bacteria.
DR HOGENOM; CLU_014322_2_1_5; -.
DR OrthoDB; 9806267at2; -.
DR Proteomes; UP000004507; 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; 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:UP000004507};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..386
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002661636"
FT DOMAIN 224..379
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
SQ SEQUENCE 386 AA; 41975 MW; 8D6D231A40E109F0 CRC64;
MIRWIVLCCL LATSAGAQAR FDPERSDIRD GWRSVQIVLG LSDIVPYRIF TLDDPRRLVL
DFQGLDTGGA SASPINSARR VTDIRFGPYR PGWTRMVLDL SEPLTLAKAE MTRDAQGAQL
TLRLARTTAD DFAAAAGAPP DPGWDALSEA ALRGLEQRQS GAFIVVLDPG HGGVDPGAER
NGITEAHLML EFAAEIAGQL RAQDGVAVVM TREADVFVPL FTRMSIARRA RADLFISLHA
DALEHDDAWG ASVYTLSEDS DDIAMELLVE RHERGDLLAG VDLSVTDDRV TGVLMDLARQ
TTSPRAASFA DHVIAQMQAQ GVRLNAKPRR TGRFSVLLAA DFPSVLIEAG FLSNTQDRQT
LTDPQSRARL VAAITQAVAQ YRSDMP
//
