ID A0A2N0UPV8_9FIRM Unreviewed; 451 AA. AC A0A2N0UPV8; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 20-JUN-2018, entry version 3. DE RecName: Full=Endolytic murein transglycosylase {ECO:0000256|HAMAP-Rule:MF_02065}; DE EC=4.2.2.- {ECO:0000256|HAMAP-Rule:MF_02065}; DE AltName: Full=Peptidoglycan polymerization terminase {ECO:0000256|HAMAP-Rule:MF_02065}; GN Name=mltG {ECO:0000256|HAMAP-Rule:MF_02065}; GN ORFNames=RB5AMG_01336 {ECO:0000313|EMBL:PKD29033.1}; OS Ruminococcus bromii. OC Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae; OC Ruminococcus. OX NCBI_TaxID=40518 {ECO:0000313|EMBL:PKD29033.1, ECO:0000313|Proteomes:UP000233562}; RN [1] {ECO:0000313|EMBL:PKD29033.1, ECO:0000313|Proteomes:UP000233562} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=5AMG {ECO:0000313|EMBL:PKD29033.1, RC ECO:0000313|Proteomes:UP000233562}; RX PubMed=29159997; RA Mukhopadhya I., Morais S., Laverde-Gomez J., Sheridan P.O., RA Walker A.W., Kelly W., Klieve A.V., Ouwerkerk D., Duncan S.H., RA Louis P., Koropatkin N., Cockburn D., Kibler R., Cooper P.J., RA Sandoval C., Crost E., Juge N., Bayer E.A., Flint H.J.; RT "Sporulation capability and amylosome conservation among diverse human RT colonic and rumen isolates of the keystone starch-degrader RT Ruminococcus bromii."; RL Environ. Microbiol. 0:0-0(2017). CC -!- FUNCTION: Functions as a peptidoglycan terminase that cleaves CC nascent peptidoglycan strands endolytically to terminate their CC elongation. {ECO:0000256|HAMAP-Rule:MF_02065}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP- CC Rule:MF_02065}; Single-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_02065}. CC -!- SIMILARITY: Belongs to the transglycosylase MltG family. CC {ECO:0000256|HAMAP-Rule:MF_02065}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:PKD29033.1}. 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; NNBY01000036; PKD29033.1; -; Genomic_DNA. DR Proteomes; UP000233562; Unassembled WGS sequence. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0008932; F:lytic endotransglycosylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule. DR HAMAP; MF_02065; MltG; 1. DR InterPro; IPR003770; YceG. DR PANTHER; PTHR30518; PTHR30518; 1. DR Pfam; PF02618; YceG; 1. DR TIGRFAMs; TIGR00247; TIGR00247; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_02065}; KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02065}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Complete proteome {ECO:0000313|Proteomes:UP000233562}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_02065, ECO:0000313|EMBL:PKD29033.1}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_02065}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_02065}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02065}. FT TRANSMEM 92 111 Helical. {ECO:0000256|HAMAP-Rule: FT MF_02065}. FT COILED 57 88 {ECO:0000256|SAM:Coils}. FT SITE 330 330 Important for catalytic activity. FT {ECO:0000256|HAMAP-Rule:MF_02065}. SQ SEQUENCE 451 AA; 51899 MW; A4C6C31E50848613 CRC64; MNPDNFNMNE QELNAQRRRR AENFKLNIDE SEYEDDNFIK SEDEPSNLNS YSGQDVKKQM ARESKQVLKQ KKKEEKKALK AKNKYNRRTF RFIWIISVLI VGAMAAVYMI TGMNDLLAVN RTDSSTVKIE IPENPTVDDV TKVLVDNKVI GEPSYFKLFV NVTKSADDFT QGTYEIRRNM DYEAIINFLS SSNNRTDTVS VTITEGESVL EIANTLEKNG ALGDRDEFLS LCNSEKFDSD FDFIKAETNA DKRYYKLEGY LYPDTYEFYR NENAESVIYK FLNNYETKIN EKQTVDGYSK KTTVLKMVEE SDTKYSLDQV MTIASIIQAE AADKEDMYYI SSILHNRLTA DSSLGVSSLG LDSTKFYPYR SLEDVPENDR STYKSRYDTY DRKGLPYGSI CNPGMDAIIA ALNPNSSDYY FFCHDSKGQA YYASTLEQQN ANLEYIESYD N //