ID   A0A1E2WPK6_9NOSO        Unreviewed;       402 AA.
AC   A0A1E2WPK6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=A4S05_33775 {ECO:0000313|EMBL:ODH00325.1};
OS   Nostoc sp. KVJ20.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Nostocaceae; Nostoc.
OX   NCBI_TaxID=457944 {ECO:0000313|EMBL:ODH00325.1, ECO:0000313|Proteomes:UP000094607};
RN   [1] {ECO:0000313|EMBL:ODH00325.1, ECO:0000313|Proteomes:UP000094607}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KVJ20 {ECO:0000313|EMBL:ODH00325.1,
RC   ECO:0000313|Proteomes:UP000094607};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-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   -!- 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:ODH00325.1}.
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DR   EMBL; LSSA01000155; ODH00325.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1E2WPK6; -.
DR   Proteomes; UP000094607; 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.
PE   4: Predicted;
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239}.
FT   DOMAIN          159..300
FT                   /note="Lytic transglycosylase MltA"
FT                   /evidence="ECO:0000259|SMART:SM00925"
SQ   SEQUENCE   402 AA;  44799 MW;  B32BE004635FB634 CRC64;
     MLVRMQSLAY SELSPPECRV KKWDIPVSLS AENQDTFPEK QKSPLIQRLP VTCCQGDSSC
     FDEVLYGEIP EKKALLSAIA RSLQYLQTAN AAAAYQNYQV AGITRDRVLK SLQRFREILL
     KTNSATELHQ AIEREFVLYQ SVGSNTKGSV LFTAYYEPLY AASRVPTAEY RYPVYRLPPD
     LKSWPRPHPT REDLEGADGL QGAKGKLRGL ELFWFRDRLE PYLAQIQGSA RLQLPDGSQT
     TIGYAGNIAY NYKSIGRELI NDGKLPLEGV TMPTILDYFQ KHPQELNIYI PRDRSFVFFQ
     ENHGEPAQGS INVPLTAERS IATDKSLMPP GALALIRASI PLVNPTGKME EQIISRYVLD
     QDAGGAIKGA GRVDYFLGTG KIAGDRAGVT VGNGQLFYLL LK
//