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Database: UniProt
Entry: T1DVA9_9HELI
LinkDB: T1DVA9_9HELI
Original site: T1DVA9_9HELI 
ID   T1DVA9_9HELI            Unreviewed;       296 AA.
AC   T1DVA9;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 25.
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=HFN_2315 {ECO:0000313|EMBL:GAD18387.1};
OS   Helicobacter fennelliae MRY12-0050.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1325130 {ECO:0000313|EMBL:GAD18387.1, ECO:0000313|Proteomes:UP000018143};
RN   [1] {ECO:0000313|EMBL:GAD18387.1, ECO:0000313|Proteomes:UP000018143}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRY12-0050 {ECO:0000313|EMBL:GAD18387.1,
RC   ECO:0000313|Proteomes:UP000018143};
RA   Rimbara E., Matsui M., Mori S., Suzuki S., Suzuki M., Kim H., Sekizuka T.,
RA   Kuroda M., Shibayama K.;
RT   "Draft Genome Sequence of Helicobacter fennelliae Strain MRY12-0050,
RT   Isolated from a Bacteremia Patient.";
RL   Genome Announc. 1:e00512-13(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:GAD18387.1}.
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DR   EMBL; BASD01000005; GAD18387.1; -; Genomic_DNA.
DR   AlphaFoldDB; T1DVA9; -.
DR   STRING; 1325130.HFN_2315; -.
DR   eggNOG; COG1559; Bacteria.
DR   Proteomes; UP000018143; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000018143};
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            185
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ   SEQUENCE   296 AA;  33559 MW;  1F5727908071D088 CRC64;
     MLIVLIVFFY LALEIKTTPI VSIPSGSISS IITYLSKNNF DINQIDKNIL RILGKPQSGL
     IDMGGERIAK GDFLYRLVNA KAAQNKIVLI PGETLYFFIQ DIAVKLSLDE NKLKESYSKY
     APYEDGVIFP NTYKIPIGIN EESLMMNLVQ QSLKIHQNLA VKLLGSYKQE EWFRYITIAS
     IIQKEAANKQ EMPLVSAVIF NRLKLKMPLQ MDGSLNYGAY SHTKITPQRI RTDPTPFNTY
     RNKGIPPYPV GSASIEAIRA AVNPADVDYL YFVRNKNGVH TFSTTYKEHL DNIHFP
//
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