ID   A0A4R0PGM6_9HYPH        Unreviewed;       363 AA.
AC   A0A4R0PGM6;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   03-MAY-2023, 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=E0D97_00695 {ECO:0000313|EMBL:TCD15994.1};
OS   Oricola cellulosilytica.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Oricola.
OX   NCBI_TaxID=1429082 {ECO:0000313|EMBL:TCD15994.1, ECO:0000313|Proteomes:UP000291301};
RN   [1] {ECO:0000313|EMBL:TCD15994.1, ECO:0000313|Proteomes:UP000291301}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 52183 {ECO:0000313|EMBL:TCD15994.1,
RC   ECO:0000313|Proteomes:UP000291301};
RX   PubMed=25566955; DOI=10.1007/s10482-014-0370-6;
RA   Hameed A., Shahina M., Lai W.A., Lin S.Y., Young L.S., Liu Y.C., Hsu Y.H.,
RA   Young C.C.;
RT   "Oricola cellulosilytica gen. nov., sp. nov., a cellulose-degrading
RT   bacterium of the family Phyllobacteriaceae isolated from surface seashore
RT   water, and emended descriptions of Mesorhizobium loti and Phyllobacterium
RT   myrsinacearum.";
RL   Antonie Van Leeuwenhoek 107:759-771(2015).
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:TCD15994.1}.
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DR   EMBL; SJST01000001; TCD15994.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4R0PGM6; -.
DR   OrthoDB; 9783686at2; -.
DR   Proteomes; UP000291301; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000291301}.
FT   DOMAIN          97..255
FT                   /note="Lytic transglycosylase MltA"
FT                   /evidence="ECO:0000259|SMART:SM00925"
SQ   SEQUENCE   363 AA;  39299 MW;  B6A4E3594AE95849 CRC64;
     MWSLRTVEFP RLPGWAEDDH SAALEALSRH FAYKHNRTYR KGAIGVDAAD LEPLHAAAAE
     SAAQKNPRSF FEAAFDAVSL QPGADERGLV TAYYEPVIAA SRERTGRFST PFYRRPADLV
     EIGEANRPPG WEDGLRFGCR SPDGTVDRYP DRATITNGWL EGRDLEIAYV EDPVDVFFAH
     VQGAARLEFA DGATTRIGYD GKNGHPFTAI GRLLAERGEI EPAEVGMASI RNWLARDRER
     GQHLMNENRS YIFFRETADE PSAGPVAAAK VPLMAGRSIA VDRLLHTFGT PVFVRADAVN
     GETWARLMIA QDTGSAIVGP ARGDLFMGSG SAAGALAGNV RSPADFHLLV PKGAVLPNPA
     GAA
//