ID A0A3G8ZTF4_9ACTN Unreviewed; 479 AA.
AC A0A3G8ZTF4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 17.
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 ECO:0000313|EMBL:AZI57754.1};
GN ORFNames=EH165_05925 {ECO:0000313|EMBL:AZI57754.1};
OS Nakamurella antarctica.
OC Bacteria; Actinomycetota; Actinomycetes; Nakamurellales; Nakamurellaceae;
OC Nakamurella.
OX NCBI_TaxID=1902245 {ECO:0000313|EMBL:AZI57754.1, ECO:0000313|Proteomes:UP000268084};
RN [1] {ECO:0000313|EMBL:AZI57754.1, ECO:0000313|Proteomes:UP000268084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14-144 {ECO:0000313|EMBL:AZI57754.1,
RC ECO:0000313|Proteomes:UP000268084};
RA Da X.;
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AZI57754.1, ECO:0000313|Proteomes:UP000268084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S14-144 {ECO:0000313|EMBL:AZI57754.1,
RC ECO:0000313|Proteomes:UP000268084};
RA Peng F.;
RT "Nakamurella antarcticus sp. nov., isolated from Antarctica South Shetland
RT Islands soil.";
RL Submitted (DEC-2018) 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 membrane {ECO:0000256|HAMAP-Rule:MF_02065};
CC Single-pass membrane protein {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; CP034170; AZI57754.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G8ZTF4; -.
DR KEGG; nak:EH165_05925; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000268084; 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; 3.30.1490.480; 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 Reference proteome {ECO:0000313|Proteomes:UP000268084};
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 97..116
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 59..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 357
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 479 AA; 50503 MW; 1ACAB79AAE811426 CRC64;
MSITTCGGRP SGRSADLADL FGHGSARAWG VPLNDNLNIF GSRDDGSEEV DVDELRRRLK
ENPTASHVLP GNRAQRSRVQ RQGRDAAKKR RRRRLRASLV ALVVLGLIGA GAALLVRSLS
SKTEVAPNYA GSGTTETIIR VRQGDGAGDI AKTLVDAGVI KSAAAYVSAA DGNTDLTRIQ
GGYYKLKQQS GVDETIAALL NPDSRVGQVD LTPGVALADF EVPANTTTGA AATVIPGYIS
QLTKAACVPL NGDSQCFTAD QLWEVAKTAD LGPKGLGLVD WAVADVTAAP DQKRRLEGMI
LPGTYNVPPG TDALAVLRSV ITESAVEWST TNIKAKAVQQ GHTTYEMAII ASIVEKEAKA
SQMPKVASVI DNRLSQTPPM KLQMDSTVNY WLSRAKISTT SGSRLDPTNL YSTYAIDGLP
PTPISAPGPD AIAATLSPAA GSWLFFVAVD LQGNSCFSVT LDEQNECIKK ARAAGVFDG
//
