ID I0ENI0_HELC0 Unreviewed; 329 AA.
AC I0ENI0;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 24-JAN-2024, entry version 42.
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 OrderedLocusNames=HCW_06195 {ECO:0000313|EMBL:AFI04499.1};
OS Helicobacter cetorum (strain ATCC BAA-429 / MIT 00-7128).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=182217 {ECO:0000313|EMBL:AFI04499.1, ECO:0000313|Proteomes:UP000005010};
RN [1] {ECO:0000313|Proteomes:UP000005010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-429 / MIT 00-7128 {ECO:0000313|Proteomes:UP000005010};
RA Kersulyte D., Berg D.E.;
RT "Complete genome sequence of Helicobacter cetorum strain MIT 00-7128.";
RL Submitted (APR-2012) 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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02065}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_02065}.
CC -!- SIMILARITY: Belongs to the transglycosylase MltG family.
CC {ECO:0000256|HAMAP-Rule:MF_02065}.
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DR EMBL; CP003479; AFI04499.1; -; Genomic_DNA.
DR RefSeq; WP_014661367.1; NC_017737.1.
DR AlphaFoldDB; I0ENI0; -.
DR STRING; 182217.HCW_06195; -.
DR KEGG; hce:HCW_06195; -.
DR PATRIC; fig|182217.3.peg.1310; -.
DR eggNOG; COG1559; Bacteria.
DR HOGENOM; CLU_025574_2_2_7; -.
DR Proteomes; UP000005010; Chromosome.
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 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 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..34
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 214
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 329 AA; 37415 MW; E2B77DF2FD54E865 CRC64;
MAHKRVSTTT KRITTLNTFL DACFLAFISI LFYLSIPISS KKIIVVPSGS LNKVLKSLQD
DGIDINQLDK ILLKLFGLPK KGYIDMGASV LRKGDFLAHL VEGKMASKSI TLIPGETRYF
FTQALSATYN IEVELLNLAY ESVAPRLNGQ VLADGVIFPD TYSLLLGQDA NRIMQTLVKQ
SMKRHETLSK EWLGYYHKEE WFEKIIIASI VQKEAANIEE MPVVASVIFN RLKKNMPLQM
DGSLNYQEFS HTKITKERVR EDNTSYNTYK FKGLPKNPVG SVSIEAIKAV IFPKETNFLY
FVKMKNKKHA FSATYKEHLN NIKISNNHF
//
