ID A0A1G6S5J8_9ACTN Unreviewed; 403 AA.
AC A0A1G6S5J8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=SAMN05421872_1066 {ECO:0000313|EMBL:SDD11476.1};
OS Nocardioides lianchengensis.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1045774 {ECO:0000313|EMBL:SDD11476.1, ECO:0000313|Proteomes:UP000199034};
RN [1] {ECO:0000313|EMBL:SDD11476.1, ECO:0000313|Proteomes:UP000199034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.6858 {ECO:0000313|EMBL:SDD11476.1,
RC ECO:0000313|Proteomes:UP000199034};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FMZM01000006; SDD11476.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6S5J8; -.
DR STRING; 1045774.SAMN05421872_1066; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000199034; Unassembled WGS sequence.
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 CDD; cd08010; MltG_like; 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 Reference proteome {ECO:0000313|Proteomes:UP000199034};
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 45..66
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 271
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 403 AA; 43003 MW; A8BEB1D270D762C5 CRC64;
MSEHHPEPDL HDDSGLLPRV DEHDEAPTYV AGGARRARKK RGRGASGCLA VLVALGVVAG
LLYFGVTAGL DKIKEQFADP EDYPGPGTGS VTFEVASGDN GSAICRNLES EGVVASVDAC
VSAVNGNPES GSIQVGFYEL QQEMASADAV ARLVDPANLL TSRVTVREGL RLTEIVDALA
EGTEFPARAY QRALRNPAAL GLPEEAGGNA EGYLFPATYD IGPDDKPVDI LKRMVDRWKQ
AAEDADLQGA AERLGYTTHE LMTIASLIEA EGRGDDMPKI SRVIYNRLEG PGDKGGTNGK
LQIDATVAYG LGLSPGSTEL TREQLDTPTP YNTRLNVVGL PPGPIEAPGD AAIKAAVEPA
DGPWYYYVTV DLATGETRFY EDYDGFLDGQ AQYKEYCETS DRC
//
