ID A0A0F5R8X7_9BACL Unreviewed; 509 AA.
AC A0A0F5R8X7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=MurNAc-LAA domain-containing protein {ECO:0000259|SMART:SM00646};
GN ORFNames=VE23_03065 {ECO:0000313|EMBL:KKC49655.1};
OS Paenibacillus sp. D9.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=665792 {ECO:0000313|EMBL:KKC49655.1, ECO:0000313|Proteomes:UP000036611};
RN [1] {ECO:0000313|EMBL:KKC49655.1, ECO:0000313|Proteomes:UP000036611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D9 {ECO:0000313|EMBL:KKC49655.1,
RC ECO:0000313|Proteomes:UP000036611};
RA Sharma V., Lin J.;
RT "Genome sequence of surfactant producing, diesel degrading Paenibacillus
RT sp. D9, isolated from diesel contaminated soil.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKC49655.1}.
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DR EMBL; JZEJ01000001; KKC49655.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F5R8X7; -.
DR PATRIC; fig|665792.3.peg.690; -.
DR Proteomes; UP000036611; Unassembled WGS sequence.
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; cd02696; MurNAc-LAA; 1.
DR Gene3D; 2.60.40.3500; -; 1.
DR Gene3D; 3.30.457.10; Copper amine oxidase-like, N-terminal domain; 1.
DR Gene3D; 3.40.630.40; Zn-dependent exopeptidases; 1.
DR InterPro; IPR012854; Cu_amine_oxidase-like_N.
DR InterPro; IPR036582; Mao_N_sf.
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; PF07833; Cu_amine_oxidN1; 2.
DR SMART; SM00646; Ami_3; 1.
DR SUPFAM; SSF55383; Copper amine oxidase, domain N; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000036611};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..509
FT /note="MurNAc-LAA domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002495366"
FT DOMAIN 395..503
FT /note="MurNAc-LAA"
FT /evidence="ECO:0000259|SMART:SM00646"
FT REGION 145..201
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..201
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 509 AA; 53398 MW; 18C1143035550613 CRC64;
MKKAAMMLVF LALFVTAFAG SASAASKTPK LYLNGQELQS ASAPRIEKDT TYIPIRTVAE
GMGFDVNWDK AAKQVSIHNG KSMIELTINK KIATVNGLSV ALPTPAKIMG AGSTSTTMVP
LRFISENMGL EVYYDSPSKS VYLYQNDASS GNGSGGATPS PAPTPTPTPT PTSTPGSGGT
GSETPTPTPT PGSGGSTAPA DATGLVTSIK YDGIGTTTIA YTGTVGDAQP FLMTGPDRIV
MDIPAASFAA DFANGFTATS AKMGEVVVDS QLLTKVRYSY YSDKPSTVRV VWDLQAAAEY
TVTKGEGTIQ LSLLGALEPV PTTPTTPSGD KIFKVVVDAG HGAHDPGAIG ISKKTEKSFN
LAIALKVNAL LKAEPRIQPI LTRSDDTFIA LDERAAIANR LNADLFISIH ANALPGSSAS
GTETYYNRAD SKTFADIVHK HLLAATGLPD RKVQTAGFVV IKKTTMPAIL TESGFLTNSK
DEAILFNEQK QNEIAQALVD GIKEYLKLS
//