ID A0A1I4NYN8_9PROT Unreviewed; 407 AA.
AC A0A1I4NYN8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=peptidoglycan lytic exotransglycosylase {ECO:0000256|ARBA:ARBA00012587};
DE EC=4.2.2.n1 {ECO:0000256|ARBA:ARBA00012587};
DE AltName: Full=Murein hydrolase A {ECO:0000256|ARBA:ARBA00030918};
GN ORFNames=SAMN05421880_10977 {ECO:0000313|EMBL:SFM20684.1};
OS Nitrosomonas nitrosa.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=52442 {ECO:0000313|EMBL:SFM20684.1, ECO:0000313|Proteomes:UP000199561};
RN [1] {ECO:0000313|EMBL:SFM20684.1, ECO:0000313|Proteomes:UP000199561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nm146 {ECO:0000313|EMBL:SFM20684.1,
RC ECO:0000313|Proteomes:UP000199561};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exolytic cleavage of the (1->4)-beta-glycosidic linkage
CC between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine
CC (GlcNAc) residues in peptidoglycan, from either the reducing or the
CC non-reducing ends of the peptidoglycan chains, with concomitant
CC formation of a 1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n1;
CC Evidence={ECO:0000256|ARBA:ARBA00001420};
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DR EMBL; FOUF01000009; SFM20684.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I4NYN8; -.
DR STRING; 52442.SAMN05421880_10977; -.
DR Proteomes; UP000199561; Unassembled WGS sequence.
DR GO; GO:0019867; C:outer membrane; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009254; P:peptidoglycan turnover; IEA:InterPro.
DR CDD; cd14668; mlta_B; 1.
DR CDD; cd14485; mltA_like_LT_A; 1.
DR Gene3D; 2.40.240.50; Barwin-like endoglucanases; 1.
DR Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR InterPro; IPR010611; 3D_dom.
DR InterPro; IPR026044; MltA.
DR InterPro; IPR005300; MltA_B.
DR InterPro; IPR036908; RlpA-like_sf.
DR PANTHER; PTHR30124; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE A; 1.
DR PANTHER; PTHR30124:SF0; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE A; 1.
DR Pfam; PF06725; 3D; 1.
DR Pfam; PF03562; MltA; 1.
DR PIRSF; PIRSF019422; MltA; 1.
DR SMART; SM00925; MltA; 1.
DR SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000199561};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..407
FT /note="peptidoglycan lytic exotransglycosylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011727917"
FT DOMAIN 143..300
FT /note="Lytic transglycosylase MltA"
FT /evidence="ECO:0000259|SMART:SM00925"
FT REGION 28..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 37..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 407 AA; 45604 MW; 60192804C80D637C CRC64;
MKNQSTLAVL AFLLGWLTAC KTDTISPAPV PTPSSPTASA KTPVNPSPSP ITPSISKLKA
VDWSQLKQWE QDTFLPAWSA FLQSCNALRN QPLWRESCNQ ANAIKQPNEN TIRHFFKHHF
IPHQVFNLDG SDEGLITGYY EPLLRGSRTP NHQYRYPLYA PPDELLIIDL GDVYPELKNL
QLRGRLEGRK VVPYYSRAEI ENNLPALKGR ELLWVDDQVE LFFLQIQGSG RIVLENGEIL
RVGYAEQNGH PYQSIGRLLV ERGELPLERA SMQGIKYWGQ QNPDKLTELL HQNSRFIFFR
ELPDNLPGPV GALGVPLTAG RSLAIDPRAV PQGAPVLLST TWPNTNQPLN RLMVAQDTGS
AIKGGVRADF FWGYGQEAAN QAGKMKQKGK MWVLLPKNYA SHLQAKK
//