GenomeNet

Database: UniProt
Entry: A0A1I4NYN8_9PROT
LinkDB: A0A1I4NYN8_9PROT
Original site: A0A1I4NYN8_9PROT 
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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system