ID A0A143Z1U3_9LACT Unreviewed; 390 AA.
AC A0A143Z1U3;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=TR210_2183 {ECO:0000313|EMBL:CZR05034.1};
OS Trichococcus ilyis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Trichococcus.
OX NCBI_TaxID=640938 {ECO:0000313|EMBL:CZR05034.1, ECO:0000313|Proteomes:UP000076878};
RN [1] {ECO:0000313|EMBL:CZR05034.1, ECO:0000313|Proteomes:UP000076878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Trichococcus_R210 {ECO:0000313|EMBL:CZR05034.1};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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}.
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DR EMBL; FJNB01000017; CZR05034.1; -; Genomic_DNA.
DR RefSeq; WP_068623719.1; NZ_FJNB01000017.1.
DR AlphaFoldDB; A0A143Z1U3; -.
DR STRING; 640938.TR210_2183; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000076878; 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; 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 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 37..61
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 274
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 390 AA; 43474 MW; 2C13EDB4A6207A2B CRC64;
MSQNEQQEPQ EPQKLIRPTL EKEAVDKMKI RKKERTLVRK IVFAIVSIGI LLGIIVGFAG
YKYITDALQP LEPESTEVVE VEIPIGTSTK GITQLLEEGK VIKNATIFNY YIKTQNVSDF
QAGFYELSPS MSLNDIIATL QAGGSPVPQS SDHKIIVREG NTAEEIAAEV EAKTDFSAEE
FLATLNDPEF LANAVAQYPE LLTEASQRTD TRYRLEGYLY PATYDYLTGN GLEEIVLQML
QKTNEVLTPY AEQIASSGHT LHEILTIASL VEKEGVTPED RANIASVFLN RLEIDMPIQS
DISILYALNE HKELVTFEDL EIDSPYNLYK NTGMGPGPFN SPSEGAIQAT LAPADTNYLY
FVADTKTGIV YFSETYDEHL QLQSQYVDSE
//
