ID A0A1V0PX59_9RHOB Unreviewed; 664 AA.
AC A0A1V0PX59;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=RGUI_2602 {ECO:0000313|EMBL:ARE40743.1};
OS Rhodovulum sp. P5.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=1564506 {ECO:0000313|EMBL:ARE40743.1, ECO:0000313|Proteomes:UP000191808};
RN [1] {ECO:0000313|EMBL:ARE40743.1, ECO:0000313|Proteomes:UP000191808}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P5 {ECO:0000313|EMBL:ARE40743.1,
RC ECO:0000313|Proteomes:UP000191808};
RA Tang K.;
RT "Shallow-sea hydrothermal system.";
RL Submitted (APR-2016) 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 -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; CP015039; ARE40743.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V0PX59; -.
DR STRING; 1564506.RGUI_2602; -.
DR KEGG; rhc:RGUI_2602; -.
DR OrthoDB; 9798982at2; -.
DR Proteomes; UP000191808; Chromosome.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR CDD; cd06583; PGRP; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 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; IPR036779; LysM_dom_sf.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
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; SSF53955; Lysozyme-like; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
DR SUPFAM; SSF47090; PGBD-like; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000191808}.
FT DOMAIN 93..236
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
FT REGION 530..551
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..544
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 664 AA; 72044 MW; 066E98EBBEF309C1 CRC64;
MPVVLAPGQV LDYRLPMLRG DMVAELQRAL IPRFLAVGED DGLFGPGTRD AVKKFQTSRR
LAATGVVDQA TARHLGDPGL SQGAVNDAAI RTVPDAHMPD ASPKRIILHW TGGGARASEL
DRKHYHFLIQ QDGTVVRGIH GIDANDRPRS GHYAAHTLNT NTKSIGISLC GMLNASERPF
RPGPAPITEN QLPVLARLVA QLCLRYGIPI TRTTVLGHGE VQSLLGIAQR QKWDPLVLPW
RTDLSFREVG DMLRSMASVE LARAQAAGDT PAEETLEEIA LRVAGTDLPG VGIVYDCATW
ARLEPLCTAM GWSHAGIEDD GVRMTAGGTE CFLPIRLLPT PDAPQGAACV RLDDLAEQLN
LSPDLSEDGA QIDLQGEIGG AVEEIGPERE RARQVTVARG DTLSRIARRE LGDAARWTEL
RDEGGRHFDS VSATRIRPGD IVLIPVAPEP AGGAAPAEVA DADVFEAFGR AAESAALVGN
GPAAREAGGR IAKACIEAGI TDLSHIAYIF ATAQHETNFG RQMVEIWRDS TQQRRYQAHP
SNAPNNPGDG KLYRGRGYVQ LTFRENYRKF GRALDLPLED RPEMVADPDI AARVLTLGMS
RVGYRSPRLV LPSFGFDGDF DFFNARRIIN ADRDKHEPRY GTSRGEGIAR HARDFRAAMS
GITI
//
