ID K2LHB4_HELPX Unreviewed; 289 AA.
AC K2LHB4;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=OUS_0996 {ECO:0000313|EMBL:EKE94164.1};
OS Helicobacter pylori R056a.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1145118 {ECO:0000313|EMBL:EKE94164.1, ECO:0000313|Proteomes:UP000006748};
RN [1] {ECO:0000313|EMBL:EKE94164.1, ECO:0000313|Proteomes:UP000006748}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R056a {ECO:0000313|EMBL:EKE94164.1,
RC ECO:0000313|Proteomes:UP000006748};
RX PubMed=23661595; DOI=10.1111/2049-632X.12045;
RA Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
RA Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
RA Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
RT "Genome sequences of 65 Helicobacter pylori strains isolated from
RT asymptomatic individuals and patients with gastric cancer, peptic ulcer
RT disease, or gastritis.";
RL Pathog. Dis. 68:39-43(2013).
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:EKE94164.1}.
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DR EMBL; AMOY01000008; EKE94164.1; -; Genomic_DNA.
DR AlphaFoldDB; K2LHB4; -.
DR PATRIC; fig|1145118.3.peg.984; -.
DR Proteomes; UP000006748; 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 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 172
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 289 AA; 32826 MW; 2737B9C0B5E54651 CRC64;
MVVVPQGSLK KVFFSLKDQG VDINALDVLF LRLMGMPKKG YIDMGDGALR KGDFLVRLIK
AKAAQKSATL IPGESRYFFT QILSETYQLE TSDLNQAYES IAPRLDGAVI EDGVILPDTY
HLPLGEDAFK IMQTLIGQSM KKHEALSKQW LGYYHKEEWF EKIILASIVQ KEAANTEEMP
LIASVIFNRL KKGMPLQMDG ALNYQEFSHA KVTKERIKTD NTPYNTYKFK GLPKNPVGSV
SLEAIKAVVF PKKTDFLYFV KMPDKKHAFS ATYKEHLKNI NLSNNHFYD
//