ID U7VF83_9FUSO Unreviewed; 318 AA.
AC U7VF83;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=HMPREF0202_00521 {ECO:0000313|EMBL:ERT69493.1};
OS Cetobacterium somerae ATCC BAA-474.
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Cetobacterium.
OX NCBI_TaxID=1319815 {ECO:0000313|EMBL:ERT69493.1, ECO:0000313|Proteomes:UP000017081};
RN [1] {ECO:0000313|EMBL:ERT69493.1, ECO:0000313|Proteomes:UP000017081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-474 {ECO:0000313|EMBL:ERT69493.1,
RC ECO:0000313|Proteomes:UP000017081};
RA Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL Submitted (AUG-2013) 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 -!- 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:ERT69493.1}.
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DR EMBL; AXZF01000019; ERT69493.1; -; Genomic_DNA.
DR RefSeq; WP_023050068.1; NZ_KI518128.1.
DR AlphaFoldDB; U7VF83; -.
DR STRING; 1319815.HMPREF0202_00521; -.
DR PATRIC; fig|1319815.3.peg.497; -.
DR eggNOG; COG1559; Bacteria.
DR HOGENOM; CLU_025574_2_0_0; -.
DR Proteomes; UP000017081; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
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; 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:UP000017081};
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 SITE 205
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 318 AA; 37072 MW; 3AA774FC4F041CE6 CRC64;
MKKKILILLF LIITIPVALF KFYSIKIEEK RDYKVQVNLK QGTSLTSVFN KLGIDKSIIF
KIFLKYEKNS GKNIKAGFYE FDGKYSYKDI LQMMEEGKVK YTILTIPEGY SIKEIGKLLQ
DRGIGTEEGL KKALENIKDF PYLTPNGNYE GYLYPETYYL SVDTNENEIV KAMTGEFLKK
FPPEKYPDKK KFYQELIMAS IIEREAQLKD EKPLMSSVFY NRLKKGMNLG SDATVNYIYD
YTKRRMYYKD LKIDSPYNTY MYKGLPPGPI SNPDYNSVMA AINPAKTDYL FFVVTSNGKH
TFTKTYKEHL EVQKKSNK
//
