ID   A0A373FSF7_COMTE        Unreviewed;       393 AA.
AC   A0A373FSF7;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   25-MAY-2022, entry version 11.
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=DZC30_04465 {ECO:0000313|EMBL:RGE46472.1};
OS   Comamonas testosteroni (Pseudomonas testosteroni).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=285 {ECO:0000313|EMBL:RGE46472.1, ECO:0000313|Proteomes:UP000261948};
RN   [1] {ECO:0000313|EMBL:RGE46472.1, ECO:0000313|Proteomes:UP000261948}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SWCO2 {ECO:0000313|EMBL:RGE46472.1,
RC   ECO:0000313|Proteomes:UP000261948};
RA   Jiang N., Zhang X.Z.;
RT   "Comamonas testosteroni strain SWCO2.";
RL   Submitted (AUG-2018) 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   -!- 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:RGE46472.1}.
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DR   EMBL; QURR01000003; RGE46472.1; -; Genomic_DNA.
DR   EnsemblBacteria; RGE46472; RGE46472; DZC30_04465.
DR   Proteomes; UP000261948; 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; cd14485; mltA_like_LT_A; 1.
DR   Gene3D; 2.40.40.10; -; 2.
DR   InterPro; IPR010611; 3D_dom.
DR   InterPro; IPR026044; MltA.
DR   InterPro; IPR034654; MltA_3D.
DR   InterPro; IPR005300; MltA_B.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   PANTHER; PTHR30124; PTHR30124; 1.
DR   Pfam; PF06725; 3D; 1.
DR   Pfam; PF03562; MltA; 1.
DR   PIRSF; PIRSF019422; MltA; 1.
DR   SMART; SM00925; MltA; 1.
DR   SUPFAM; SSF50685; SSF50685; 1.
PE   4: Predicted;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..393
FT                   /note="Peptidoglycan lytic exotransglycosylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5016953543"
FT   DOMAIN          145..284
FT                   /note="MltA"
FT                   /evidence="ECO:0000259|SMART:SM00925"
FT   REGION          25..58
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   393 AA;  43443 MW;  B92984E36E92F9EB CRC64;
     MNVHLLRRAS LALIVATLVA CTTTKQQNDP SAVPELQPHG GGAASTTQKP PFTANVPTKS
     RWVPVDWGDL PGVATDSLNE AWNAWIKNCE RPSTTFASLC SDVRRMSIAS EDEQRKWMMT
     HLQPYRIEAT TGSPDGMLTS YYEPMYEARR VQGNGFNVPI YQTPRGFGQR KPWYTRQQID
     TNAEAQAALS GRVIAWLRDP VDMLVLHIQG SGRLQLTEAN GTQRMIRVAY AGTNDQPYKS
     VGRWLLDQGL VRDATWPGIS AWIASNPSRV NEMLWSNPRY VFFKEEELNE FDAQFGPKGA
     QGVALTPGRS IAVDRNSIPY GTPVWLSTPG PTVALNRLVF AQDTGSAIVG AVRADYFMGW
     GAEAGDVAGR IKQPLKLWAF WPKSLAGSAP HLR
//