ID A0A2M8T6V1_9CLOT Unreviewed; 339 AA.
AC A0A2M8T6V1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
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=CUB90_01820 {ECO:0000313|EMBL:PJI06681.1};
OS Clostridium sp. CT7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=2052574 {ECO:0000313|EMBL:PJI06681.1, ECO:0000313|Proteomes:UP000230839};
RN [1] {ECO:0000313|EMBL:PJI06681.1, ECO:0000313|Proteomes:UP000230839}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT7 {ECO:0000313|EMBL:PJI06681.1,
RC ECO:0000313|Proteomes:UP000230839};
RA Xin F., Chen T.;
RT "The draft genome sequence of Clostridium sp. CT7, a unique bacterium
RT capable of producing butanol from glycerol uncoupled acetone and 1,3-
RT propanediol formation.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- 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 -!- 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:PJI06681.1}.
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DR EMBL; PETE01000002; PJI06681.1; -; Genomic_DNA.
DR RefSeq; WP_066019596.1; NZ_PETE01000002.1.
DR AlphaFoldDB; A0A2M8T6V1; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000230839; Unassembled WGS sequence.
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; 3.30.160.60; Classic Zinc Finger; 1.
DR Gene3D; 3.30.1490.480; Endolytic murein transglycosylase; 2.
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:UP000230839};
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 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 225
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 339 AA; 38700 MW; 3B98535263311A59 CRC64;
MNLKTVLKKK FYILLFLVLI LIFSAGVYFN YSMNHPFKVK DNVSFQINNG DNLYSVVSKL
KSQNLIKSKF VLKLYIKYKK VPGDIKPGLY SIKKGESSRE FLNDIRYGNF DSSYVKVTIP
EGYDIEQIAN LLDKKGLISK KNFIKACEDY KAPGYIKSDK DRKYNLEGYL FPDTYAFKKG
SSGKELIDVM IKKFNEVFKK AEKETGKSTQ NVDETITMAS IIEREAKVNS ERPIIASVFF
NRLKINMKLQ SCATVEYSLG YHKDKLSNED LKVNSKYNTY LINGMPVGPI CSPGKASIEA
ALNPSKTNYI YFVSNNNGTH TFTSNYNEFL KAKKKTQGF
//
