ID X2JRJ3_AGGAC Unreviewed; 347 AA.
AC X2JRJ3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=CF65_00305 {ECO:0000313|EMBL:AHN70921.1};
OS Aggregatibacter actinomycetemcomitans HK1651.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Aggregatibacter.
OX NCBI_TaxID=272556 {ECO:0000313|EMBL:AHN70921.1, ECO:0000313|Proteomes:UP000019758};
RN [1] {ECO:0000313|EMBL:AHN70921.1, ECO:0000313|Proteomes:UP000019758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK1651 {ECO:0000313|EMBL:AHN70921.1,
RC ECO:0000313|Proteomes:UP000019758};
RA Gillaspy A.F., Griffin J., Najar F., Hinkle J., Lewis L.A.,
RA McLaughlin R.E., Hartman K., Nydick C., Gipson M., Conway B., Vaughn J.,
RA Thompson C., Gipson J., Maddera L., Carson M., Kenton S., Lai H., Roe B.A.,
RA Orvis J., Zaitshik J., Griffin J., Scott E., Dyer D.W.;
RT "Genome sequencing and closure of the periodontal pathogen, Aggregatibacter
RT actinomycetemcomitans.";
RL Submitted (MAR-2014) 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}.
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DR EMBL; CP007502; AHN70921.1; -; Genomic_DNA.
DR RefSeq; WP_005567730.1; NZ_CP007502.1.
DR AlphaFoldDB; X2JRJ3; -.
DR SMR; X2JRJ3; -.
DR GeneID; 77210650; -.
DR KEGG; aah:CF65_00305; -.
DR PATRIC; fig|272556.10.peg.216; -.
DR eggNOG; COG1559; Bacteria.
DR HOGENOM; CLU_025574_0_2_6; -.
DR Proteomes; UP000019758; Chromosome.
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; 2.
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 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 225
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 347 AA; 39932 MW; BEC175F4120B7ACF CRC64;
MKKFCLFLLF LLVLLAGAGF WGYRQLQQFV QQPVNVQKDR LFTVERGTTG SKLVTLLQNE
HLLENAALLP WVLKIYPEFN KVKAGTYALD NVKTVEDLLK LLNSGKEAQF NVQFIEGNTF
KTWRKRLENA PHLKQTLKDK SEQEIFHLLA IPDVAQEVYE WLKIEGWLYP DTYNYTPNST
DLELLQRSAE RMKKALDKAW QERDKDLPLA NPYEMLILAS IVEKETGIAA ERPQVASVFI
NRLKAKMKLQ TDPTVIYGMG DDYNGNIRKK DLETPTPYNT YVIDGLPPTP IAMPSEEALQ
AVAHPAQTAF YYFVADGTGG HKFSRNLNEH NKAVQQYLRW YREQNGK
//
