ID D7GDR5_PROFC Unreviewed; 410 AA. AC D7GDR5; DT 10-AUG-2010, integrated into UniProtKB/TrEMBL. DT 10-AUG-2010, sequence version 1. DT 02-OCT-2024, entry version 67. DE RecName: Full=Endolytic murein transglycosylase {ECO:0000256|HAMAP-Rule:MF_02065}; DE EC=4.2.2.29 {ECO:0000256|HAMAP-Rule:MF_02065}; DE AltName: Full=Peptidoglycan lytic transglycosylase {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 OrderedLocusNames=PFREUD_11540 {ECO:0000313|EMBL:CBL56676.1}; OS Propionibacterium freudenreichii subsp. shermanii (strain ATCC 9614 / DSM OS 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1). OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales; OC Propionibacteriaceae; Propionibacterium. OX NCBI_TaxID=754252 {ECO:0000313|EMBL:CBL56676.1, ECO:0000313|Proteomes:UP000000936}; RN [1] {ECO:0000313|EMBL:CBL56676.1, ECO:0000313|Proteomes:UP000000936} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 9614 / DSM 4902 / CIP 103027 / NCIMB 8099 / CIRM-BIA1 RC {ECO:0000313|Proteomes:UP000000936}; RX PubMed=20668525; DOI=10.1371/journal.pone.0011748; RA Falentin H., Deutsch S.M., Jan G., Loux V., Thierry A., Parayre S., RA Maillard M.B., Dherbecourt J., Cousin F.J., Jardin J., Siguier P., RA Couloux A., Barbe V., Vacherie B., Wincker P., Gibrat J.F., Gaillardin C., RA Lortal S.; RT "The complete genome of Propionibacterium freudenreichii CIRM-BIA1, a hardy RT actinobacterium with food and probiotic applications."; RL PLoS ONE 5:E11748-E11748(2010). CC -!- FUNCTION: Functions as a peptidoglycan terminase that cleaves nascent CC peptidoglycan strands endolytically to terminate their elongation. CC {ECO:0000256|HAMAP-Rule:MF_02065}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a peptidoglycan chain = a peptidoglycan chain with N- CC acetyl-1,6-anhydromuramyl-[peptide] at the reducing end + a CC peptidoglycan chain with N-acetylglucosamine at the non-reducing CC end.; EC=4.2.2.29; Evidence={ECO:0000256|HAMAP-Rule:MF_02065}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_02065}; CC Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_02065}. CC -!- SIMILARITY: Belongs to the transglycosylase MltG family. CC {ECO:0000256|HAMAP-Rule:MF_02065}. 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; FN806773; CBL56676.1; -; Genomic_DNA. DR RefSeq; WP_013161050.1; NC_014215.1. DR AlphaFoldDB; D7GDR5; -. DR STRING; 754252.PFREUD_11540; -. DR KEGG; pfr:PFREUD_11540; -. DR eggNOG; COG1559; Bacteria. DR HOGENOM; CLU_025574_4_0_11; -. DR Proteomes; UP000000936; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. 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 CDD; cd08010; MltG_like; 1. DR Gene3D; 3.30.1490.480; Endolytic murein transglycosylase; 1. DR HAMAP; MF_02065; MltG; 1. DR InterPro; IPR003770; MLTG-like. DR NCBIfam; TIGR00247; endolytic transglycosylase MltG; 1. DR PANTHER; PTHR30518:SF2; ENDOLYTIC MUREIN TRANSGLYCOSYLASE; 1. DR PANTHER; PTHR30518; UNCHARACTERIZED; 1. DR Pfam; PF02618; YceG; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_02065}; KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316, KW ECO:0000256|HAMAP-Rule:MF_02065}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_02065}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02065}; KW Reference proteome {ECO:0000313|Proteomes:UP000000936}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_02065}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_02065}. FT TRANSMEM 63..86 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065" FT REGION 1..55 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..20 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT SITE 284 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065" SQ SEQUENCE 410 AA; 43846 MW; 2413B8CA6BCC46AD CRC64; MAGPKRAADE DAEDLYLPAS RGEEPEPIRS GAATEGPHGP AASGGEQPPL ITMTRDYHRT PGSWLKSVIA VLVSLAVIGG GGFLIYHKVT EYQGADYTGA GQSDVTVTVK SGESVSQMGD LLVAEDVVAS RNAFMRAAKK EKRTNNIQAG TYKMKTRMPA ADVVAVLVDP SNIVNNRFTV PEGLRNTHVL EQVSSATGIA LGQLTAASKD PSLPVPSYAQ GSSEGFLFPD TYTFEPDFTA SQVLTRMVDR FNQVAADENL EKRAAAAGRS PHDVLVVASI IERETSDHKY APLVAEVIYN RLAQGMRLQS DATVAYANNL EGKVTTTDEE RGLNSPYNTY MVDGLPPTPI SNPGKAAIDA ALAPASGDYL YFVTVNLDTG ETKFASDSAG HDQNVKEFQT WCQANSDHCK //