ID A0A416RF21_9FIRM Unreviewed; 374 AA.
AC A0A416RF21;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, 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 ECO:0000313|EMBL:RHR11021.1};
GN ORFNames=DWX58_00745 {ECO:0000313|EMBL:RHR11021.1};
OS Pseudoflavonifractor sp. AF19-9AC.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Pseudoflavonifractor.
OX NCBI_TaxID=2292244 {ECO:0000313|EMBL:RHR11021.1, ECO:0000313|Proteomes:UP000285063};
RN [1] {ECO:0000313|EMBL:RHR11021.1, ECO:0000313|Proteomes:UP000285063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF19-9AC {ECO:0000313|EMBL:RHR11021.1,
RC ECO:0000313|Proteomes:UP000285063};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-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}.
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:RHR11021.1}.
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DR EMBL; QUGI01000001; RHR11021.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A416RF21; -.
DR Proteomes; UP000285063; 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 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:UP000285063};
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 31..57
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 255
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 374 AA; 41988 MW; AC75255DD8857486 CRC64;
MAQERRTRQT SEQPSSSRPQ RRSRRRSTGS TISFAALYVI GVIGVSILLA CIGWIAANDV
LALNKPEKEV VFTISSEDTF NDVVDHLEEE GLIEYKLLFK LFATFTHGKD KVTMGTYTLN
TDMDYRALLS GMSIYSSSRA EVTITIPEGY TLAQIFQLLE DKGVSTVEDL NEAAANHDYA
FSFLQDIPLG DPIRLEGFLY PDTYNFYTPH DPVYAINKML VNFDAKYTDE LRQQVADSGY
SIREILTIAS MIERETDGSD RGTISSVIYN RLDNPDAGTM GYLQIDATLA YINGGKVPTA
ADKEIDSPYN TYKYKGLPPA PIANPGLEAI KAALDPEDTS YFYYTLGDDE KHHFFKTYNE
MQSFMATQEL YKSN
//
