ID A0A271JDY2_9BACT Unreviewed; 354 AA.
AC A0A271JDY2;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
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=B1759_08025 {ECO:0000313|EMBL:PAP81274.1};
OS Rubrivirga sp. SAORIC476.
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Rubricoccaceae;
OC Rubrivirga.
OX NCBI_TaxID=1961794 {ECO:0000313|EMBL:PAP81274.1, ECO:0000313|Proteomes:UP000216627};
RN [1] {ECO:0000313|EMBL:PAP81274.1, ECO:0000313|Proteomes:UP000216627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAORIC476 {ECO:0000313|EMBL:PAP81274.1,
RC ECO:0000313|Proteomes:UP000216627};
RA Kumagai Y., Kogure K., Yoshizawa S.;
RT "Whole genome sequence of Rhodothermus Rubrivirga sp. SAORIC476.";
RL Submitted (FEB-2017) 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:PAP81274.1}.
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DR EMBL; MVOI01000003; PAP81274.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A271JDY2; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000216627; 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 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 212
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 354 AA; 39559 MW; 75C92A212FB080FC CRC64;
MKKLFLLVLA IGALAAGAVW WFAFSSNVGG TERHSVRIPE GTGFEAALDS LESADALANR
SSMELFGRLT GWADQVKTGH YYIEPGMSNW AVLDKIRKGL QDPIRITIPP GSRPERTARV
LRNQLGTDST EVARLLRDPA FAESLGTDVA HLHGQMLAET FDMYWTDDAE TALRRIHERY
DRFWTDARRA KADALGLTPD EVVTLASLVE WEARKPEERR RIAGLYLNRL LGRTSAGTMR
LQADPTVQFA LMEEGGEPQM RRLFFSDYAF PSAYNTYLID GLPPGPITNP SDGTVEAVLD
NESHDFLFFV ADGTGGHDFS RTVAEHNAKA ARWSQYLQEQ TRIRRQREAA EASP
//