ID A0A2N8LBN9_9STRE Unreviewed; 610 AA.
AC A0A2N8LBN9;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=AT575_06670 {ECO:0000313|EMBL:PND47562.1};
OS Streptococcus penaeicida.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1765960 {ECO:0000313|EMBL:PND47562.1, ECO:0000313|Proteomes:UP000235963};
RN [1] {ECO:0000313|EMBL:PND47562.1, ECO:0000313|Proteomes:UP000235963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 1838 {ECO:0000313|EMBL:PND47562.1,
RC ECO:0000313|Proteomes:UP000235963};
RA Gomez-Gil B., Morales-Covarrubias M.;
RT "Streptococcus penaeicida sp. nov.";
RL Submitted (DEC-2015) 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:PND47562.1}.
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DR EMBL; LOCM01000024; PND47562.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N8LBN9; -.
DR Proteomes; UP000235963; 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 244..268
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 71..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..120
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 487
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 610 AA; 68267 MW; C07007D8C24AF39C CRC64;
MTDFKDDGQE SQKKMSFKEH ILAELEKANQ IRKEKEEELL QQDLKAEELK LKEREAEEAR
QKTVALYNDY QEEMAKSVEN SQDSVHESEQ ETENQSEMDA NESLLGFEES SVSSESEVLE
TSEIDGSEDF DSQSFSHSES VIQSDDSQEL EKDSLVGSDL SETIPFTPIT ILNPADIGVA
LEDNQEEETR ESRPSQPIQE EQAHFTSDID INHDEASEAS HTVGGLVKKR NSKRQETDRV
AKKISMVLIS SILAIIVIIA LATSLFVYNA VNPVDKKDDK YVQVEIPAGS GNKLIGQVLE
ENGLIKSGTV FNFYTKFKNF SNFQSGYYNL QKSMSLDEIA RALQKGGNDK PTKPVLGKIL
IPEGYTIKQI SKAVTDNSNT KSTKDKTPFK SQDFLNLIQD ETFIKEMVKK YPRLLSSLPK
KEDAVYQLEG YLFPATYDYY KDTDIRSLVD EMLATTDATL SPYYDSIEAS GKTVNEVLTL
ASLVEKEGST DEDRRDIASV FYNRLQNGMA LQSNIAILYA MNKLGDKTTL AEDAAIDTTI
KSPYNIYTNT GLMPGPVDSP SLSAIDATVK PANTDYLYFV ANVKTGEVFY AKTYEAHSAN
VEKYVNNQIQ
//
