ID A0A1G9K261_9FIRM Unreviewed; 346 AA.
AC A0A1G9K261;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
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=SAMN04488692_104144 {ECO:0000313|EMBL:SDL43435.1};
OS Halarsenatibacter silvermanii.
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halarsenatibacteraceae;
OC Halarsenatibacter.
OX NCBI_TaxID=321763 {ECO:0000313|EMBL:SDL43435.1, ECO:0000313|Proteomes:UP000199476};
RN [1] {ECO:0000313|EMBL:SDL43435.1, ECO:0000313|Proteomes:UP000199476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SLAS-1 {ECO:0000313|EMBL:SDL43435.1,
RC ECO:0000313|Proteomes:UP000199476};
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 -!- SIMILARITY: Belongs to the transglycosylase MltG family.
CC {ECO:0000256|HAMAP-Rule:MF_02065}.
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DR EMBL; FNGO01000004; SDL43435.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9K261; -.
DR STRING; 321763.SAMN04488692_104144; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000199476; 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 Reference proteome {ECO:0000313|Proteomes:UP000199476};
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 233
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 346 AA; 40355 MW; CD482F98162760F4 CRC64;
MKKAGIIFLI LLMTASLYLW FDHHRRPAEE WQEKSAEERR VEVSAGSSLE EIADKLFDEG
VIRSRHLFKI YARLHEMDRN MQAGLYKFSR NQKVDEIVEK IGQGRVYTER LAVPEGSTVE
EIASRAASNL KLTEDEFLQE ARRSADGRNY LPDSDSLQYR IEGFLYPTTY LVPYDIDPGD
LIDTMLDRFE EKWLDEIESF IYERDDFKES WMDFQENWTI REVVVLASLI EKEAVLPEEK
PVIAGVILNR LKDNMRLQID ATVQYALTER KERLLYSDLE VDSPYNTYLY PGLPPGPIAS
PGDEAIKAAI EPDKNDYLFF FARGDGSHEF TKSYQEHLQR QRKLLD
//
