ID A0A1G7U6M3_9SPHI Unreviewed; 350 AA.
AC A0A1G7U6M3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=SAMN05192573_103386 {ECO:0000313|EMBL:SDG43018.1};
OS Mucilaginibacter gossypii.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=551996 {ECO:0000313|EMBL:SDG43018.1, ECO:0000313|Proteomes:UP000199705};
RN [1] {ECO:0000313|EMBL:SDG43018.1, ECO:0000313|Proteomes:UP000199705}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gh-67 {ECO:0000313|EMBL:SDG43018.1,
RC ECO:0000313|Proteomes:UP000199705};
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; FNCG01000003; SDG43018.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7U6M3; -.
DR STRING; 551996.SAMN05192573_103386; -.
DR Proteomes; UP000199705; 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; 3.30.160.60; 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 TRANSMEM 14..35
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 225
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 350 AA; 39826 MW; FD9F3042D0CC0028 CRC64;
MTAEKQGSGM LKKIIIALVI IIVVLLGFTG FNYYLKYFGP NVTDKQEYLY IHTGATFGDV
FKTIQDEGTV KDTASFGWAA RNMNYITRVK PGKYRLHEGM GNRKLINMLA SGTQEPVRVE
FHGLRLKEQF AGFISKKIEP DSMAIIRLLD SASFVSKYGF TTDNVYTVIM PDSYQMYWNT
SPEKFFKRMY DHYQAFWTPE RKQLAAAINL TPQEVSVLAS IVDAEALHDD EMPAVAGLYL
NRLKKGMKLE ADPTVIFALN DFTIKRVLTR YLSYNSPYNT YLHTGLPPGP IMMPSVNAVK
AVLNYQKSDY IYMCAKADFS GYHAFATNVA DHLVNAHKFQ QALNERNIRR
//
