ID A0A3N5CXZ8_9SPHN Unreviewed; 323 AA.
AC A0A3N5CXZ8;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 14.
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:RPF72510.1};
GN ORFNames=EG799_13395 {ECO:0000313|EMBL:RPF72510.1};
OS Aurantiacibacter spongiae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Aurantiacibacter.
OX NCBI_TaxID=2488860 {ECO:0000313|EMBL:RPF72510.1, ECO:0000313|Proteomes:UP000275232};
RN [1] {ECO:0000313|EMBL:RPF72510.1, ECO:0000313|Proteomes:UP000275232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HN-E23 {ECO:0000313|EMBL:RPF72510.1,
RC ECO:0000313|Proteomes:UP000275232};
RA Zhuang L., Luo L.;
RT "Erythrobacter spongiae sp. nov., isolated from a marine sponge.";
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:RPF72510.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; RPFZ01000001; RPF72510.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N5CXZ8; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000275232; 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 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:UP000275232};
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 199
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 323 AA; 34744 MW; 52D1493F0E358F75 CRC64;
MTRTFGLLAA VGVLIVAVLA GWFLAGWYGS AEIEEDTAFI VPSGATLTST ANKLAQVGVI
GDADGFLLRA KLLGSGDPVK AGEFMLAAND SPAGILDTLQ HGEVIRRFVT VPEGMPSVMV
HDILMAEPLL TGAIPVPEEG SVLPDTYDFE RGESRAAVLA RMQVAMDRAV AELWPRRSPD
TVAKTPQEAV TLASIVEKET GVPRERRMVA GLYSNRIRQG IRLQADPTII YPITKGRPLG
RRIRQSEIAA INDYNTYSMA GLPKGPITNP GRASIEAVLH PADTDAIYMV ADGTGGHEFN
DTLAGHNAAV ERWFALRRER GEM
//
