ID A0A1S2LVQ6_9BACI Unreviewed; 375 AA.
AC A0A1S2LVQ6;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, 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 ORFNames=BKP37_05145 {ECO:0000313|EMBL:OIJ16621.1};
OS Anaerobacillus alkalilacustris.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anaerobacillus.
OX NCBI_TaxID=393763 {ECO:0000313|EMBL:OIJ16621.1, ECO:0000313|Proteomes:UP000179524};
RN [1] {ECO:0000313|EMBL:OIJ16621.1, ECO:0000313|Proteomes:UP000179524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18345 {ECO:0000313|EMBL:OIJ16621.1,
RC ECO:0000313|Proteomes:UP000179524};
RA Bassil N.M., Lloyd J.R.;
RT "Draft genome sequences of four alkaliphilic bacteria belonging to the
RT Anaerobacillus genus.";
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}.
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:OIJ16621.1}.
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DR EMBL; MLQR01000004; OIJ16621.1; -; Genomic_DNA.
DR RefSeq; WP_071308605.1; NZ_MLQR01000004.1.
DR AlphaFoldDB; A0A1S2LVQ6; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000179524; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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 31..54
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT COILED 1..28
FT /evidence="ECO:0000256|SAM:Coils"
FT SITE 262
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 375 AA; 43445 MW; 073AE50A36A0111D CRC64;
MEKEEKKKQK LEIKRKKLQE RQEEASIVRK IVLACLLFII IALGIAGTSA YYYVKSSLGP
MDETDEEMID IHIPIGSTST RIGNILEENG LINNSSFFRY YIRYRNESGF QAGDYQLSKS
MTMDEIIVAL KEGTLLQDYA VSFTIPEGRW LENILKTISE NTNHELKDLE EKVKDEQYLK
ELINRYTVLT EDIINEEIRW PLEGYLFPAR YDFVEENPSI ETIIESMLTR TEQVVGRYFD
DLEDSEYTTH EILTLASIIE GEAQKSEDRY KISGVLYNRL NQNMRLEVDP TVAYAHGEHL
SRTLYAHLEI NSPYNTYRIT GIPVGPINNP GEASIKAALQ PAEHNDLFFY ATNEGNVIYS
ETFQQHQEVL REYRD
//
