ID A0A4R0PGM6_9HYPH Unreviewed; 363 AA. AC A0A4R0PGM6; DT 31-JUL-2019, integrated into UniProtKB/TrEMBL. DT 31-JUL-2019, sequence version 1. DT 02-OCT-2024, entry version 13. 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 Ahrensiaceae; 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}. 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; 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 //