ID A0A2S0PAU1_9NEIS Unreviewed; 631 AA.
AC A0A2S0PAU1;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Peptidoglycan N-acetylmuramoylhydrolase {ECO:0000313|EMBL:AVY94455.1};
GN ORFNames=DAI18_10645 {ECO:0000313|EMBL:AVY94455.1};
OS Microvirgula aerodenitrificans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Aquaspirillaceae; Microvirgula.
OX NCBI_TaxID=57480 {ECO:0000313|EMBL:AVY94455.1, ECO:0000313|Proteomes:UP000244173};
RN [1] {ECO:0000313|EMBL:AVY94455.1, ECO:0000313|Proteomes:UP000244173}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BE2.4 {ECO:0000313|EMBL:AVY94455.1,
RC ECO:0000313|Proteomes:UP000244173};
RA Anderson E., Jang J., Ishii S.;
RT "Denitrifier Microvirgula.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
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DR EMBL; CP028519; AVY94455.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S0PAU1; -.
DR STRING; 1122240.GCA_000620105_00162; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000244173; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR CDD; cd00118; LysM; 3.
DR CDD; cd16894; MltD-like; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 3.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR000189; Transglyc_AS.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR PANTHER; PTHR33734; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 2; 1.
DR PANTHER; PTHR33734:SF22; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE D; 1.
DR Pfam; PF01476; LysM; 3.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00257; LysM; 3.
DR SUPFAM; SSF54106; LysM domain; 3.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51782; LYSM; 3.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:AVY94455.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244173};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..631
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015558713"
FT DOMAIN 320..363
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 517..560
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 583..627
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 631 AA; 68596 MW; 3633FE9A8B6B4366 CRC64;
MKHTLKLALS LAFAGGLAGQ AHAEFDNLSY SSGQAMMQQN NILLRNGDDV WQRIREGFQM
DEVNADLVRR FERQYAANPA GIERTLGRSH KYLFHIINEV EKRGMPTELA LLPVVESAFV
PQAESPVGAA GLWQFMPATG RHYGLEQTWW YDGRRDVVGA TQAALNYLEY LHGLFGDWSL
ALAAYNWGEG NVSRAQERNR AQGLPDDFEH IRMPAETRNY VPKLIAVRNV LSDPKRYNVA
LNKFPNRPYF VAVSTGKHID IDVAAKLANV PEAELKTLNP GYKRPLLAYK NGRQLLIPVD
HFDRFEKNLA SWDKPLSQWQ AVVAQDGDTP DVVAERYNMT VAELRSVNGA LGGRLQAGQP
LLVAQRGSSA APALIAAADR DDQAEAPRTV AARPVSDSPA RPVVTVARAP VVADKAPVMA
AAPVARPAVM VASADTRPAA SSRSSSAVTT DLPPAVDTVA SPRPFADIEV VPSPVVATAA
SAEDAISEIA SIRPAVDTVA RTEPARPQQT AAVATSSRHT VSSGDTLYSL AKRYNMSVAQ
LRDLNQLNGN ALQLGQTLQV AAGSSDLITV AASSAAAPRT QQYQYVVQRG DTLYSIARKF
GLDHQDLRRW NDERKLARLQ PGNRVTLVVG I
//
