ID A0A0D0IU82_9MICO Unreviewed; 366 AA.
AC A0A0D0IU82;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=SD72_06055 {ECO:0000313|EMBL:KIP53073.1};
OS Leucobacter komagatae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leucobacter.
OX NCBI_TaxID=55969 {ECO:0000313|EMBL:KIP53073.1, ECO:0000313|Proteomes:UP000032120};
RN [1] {ECO:0000313|EMBL:KIP53073.1, ECO:0000313|Proteomes:UP000032120}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM ST2845 {ECO:0000313|EMBL:KIP53073.1,
RC ECO:0000313|Proteomes:UP000032120};
RA Karlyshev A.V., Kudryashova E.B.;
RT "Draft genome sequence of Leucobacter komagatae strain VKM ST2845.";
RL Submitted (JAN-2015) 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:KIP53073.1}.
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DR EMBL; JXSQ01000005; KIP53073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D0IU82; -.
DR Proteomes; UP000032120; 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; 3.30.1490.480; 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:UP000032120};
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..35
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 234
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 366 AA; 39853 MW; F4B9467F9C416871 CRC64;
MSEEDRRSRK RGRIVISSVL IVMLLLVGGG AALMWNTYGE RISLALGWSS NDYEGQGSGE
VLLTISSGQF GADVAEALAQ ADVVKSSEAF YDLLLQQEEE VSFQVGTYRL KHQMSAKAAL
AALQDEANRM ELTVTIPEGT AALDALELTA GVVDIPFDDF KKAAADPAAF GVPSEFPSIE
GFLFPATYTF EPGDTAETII QTMVDRMWQA LRDHGVAEGD AWEVLTLAAM VQREAGSRLE
DFPKVARVFL NRIDIDMLLQ SDATVSYGTG NTHTVWTTDE ERADKSNKYN TYANQGLPAG
PIGLPGDTAI EAATNPADGP WLYFMPVDLS SGETEFAETI EEHDQNVQKL ADWCTTHRAE
GGKYCD
//
