ID A0A3N5Y3D9_9ALTE Unreviewed; 338 AA.
AC A0A3N5Y3D9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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 ECO:0000313|EMBL:RPJ67306.1};
GN ORFNames=DRW07_07175 {ECO:0000313|EMBL:RPJ67306.1};
OS Alteromonas sediminis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=2259342 {ECO:0000313|EMBL:RPJ67306.1, ECO:0000313|Proteomes:UP000275281};
RN [1] {ECO:0000313|EMBL:RPJ67306.1, ECO:0000313|Proteomes:UP000275281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U0105 {ECO:0000313|EMBL:RPJ67306.1,
RC ECO:0000313|Proteomes:UP000275281};
RA Ye M.-Q., Du Z.-J.;
RL Submitted (NOV-2018) 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:RPJ67306.1}.
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DR EMBL; RPOK01000002; RPJ67306.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N5Y3D9; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000275281; 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 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 inner membrane {ECO:0000256|HAMAP-Rule:MF_02065};
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:UP000275281};
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 220
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 338 AA; 37315 MW; 89EFA86F1B7517CB CRC64;
MIARILLGTA GILVMLSLLT GLWYKSQIAH PLGIDNGTLL AVSGGDTPHS VLKDLLAKSD
HDLPVLVGKI WIKTALGKKP IQKGIYEIDA TMTIEQVYAL LQSGKQKQFS ITLVEGLTFK
DWLGQLKQAP YLHDDWNEET SELLMDKLYK TLELEVSSWE GLLLAETYAY TAHSKISDIV
VRAANALHNA LGLIQSSFPL PNELNSQYEA LILASIVEKE TAQPDERALI SGVFLNRLAL
GMKLQTDPTV IYGIGEGFDG DITRAHLRQA TPYNTYVIKG LPPTPIAMVG REALQAVYQP
MPTEFLYFVA KGDGTHQFSK TLAEHNKAVR KYQLGINE
//
