ID A0A2S7SWN6_9BACT Unreviewed; 341 AA.
AC A0A2S7SWN6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, 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:PQJ11021.1};
GN ORFNames=CJD36_013715 {ECO:0000313|EMBL:PQJ11021.1};
OS Flavipsychrobacter stenotrophus.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavipsychrobacter.
OX NCBI_TaxID=2077091 {ECO:0000313|EMBL:PQJ11021.1, ECO:0000313|Proteomes:UP000239872};
RN [1] {ECO:0000313|EMBL:PQJ11021.1, ECO:0000313|Proteomes:UP000239872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RB1R16 {ECO:0000313|EMBL:PQJ11021.1,
RC ECO:0000313|Proteomes:UP000239872};
RA Liu Q., Xin Y.-H.;
RT "A novel member of the phylum Bacteroidetes isolated from glacier ice.";
RL Submitted (JAN-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:PQJ11021.1}.
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DR EMBL; PPSL01000003; PQJ11021.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7SWN6; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000239872; 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:UP000239872};
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 217
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 341 AA; 38271 MW; 1E87B9C989B09885 CRC64;
MSAKKKKKSR LPLIITIVVI VLLLGAAYKI LGPNSGKAQF LYIRTGITYE QLLTQMKDGG
YVNDINSFDF LAKRAGLPEH IHPGKYQMKW GMTNYELVKK LRNGRQVPVK LVINKLRTKA
DFIRLVSTNL EIDSLQLGAL MRDKDFLDKM GLDSNTVMCG VRPDTYEFYW NTTTDKLFKK
LKESYSRFWT DARREQAKNH GLNPVKATIM ASIIDEETNL PADKLNIASV YLNRMDKGMK
LQADPTVKFS IGDFTIKRVT GAMLKTESPY NTYQNVGLPP GPICTPSNGS IDAVLNAPQT
TYIYFCAKAD LSGASVFATT DAEHLLNARL YQQALNARGI H
//
