ID A0A1H3KBS1_9BACI Unreviewed; 387 AA.
AC A0A1H3KBS1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, 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 ORFNames=SAMN05421736_10293 {ECO:0000313|EMBL:SDY49048.1};
OS Evansella caseinilytica.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Evansella.
OX NCBI_TaxID=1503961 {ECO:0000313|EMBL:SDY49048.1, ECO:0000313|Proteomes:UP000198935};
RN [1] {ECO:0000313|Proteomes:UP000198935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SP {ECO:0000313|Proteomes:UP000198935};
RA Varghese N., Submissions S.;
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; FNPI01000002; SDY49048.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3KBS1; -.
DR STRING; 1503961.SAMN05421736_10293; -.
DR Proteomes; UP000198935; 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};
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:UP000198935};
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 40..60
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 269
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 387 AA; 44450 MW; 940D0D6A09DC6777 CRC64;
MTEDNKRAKN DLQKDKSKLK AINAGKLEEK QKEAGLVRKI VLITFIVIVL SLAGAAYGTY
KYVMNALSPV DENDDEIIEV TIPIGSSTTG IADVLKENGL ISNASVFRYY VKFKNESGFQ
AGDYELSRSM SVDRIIDELK HGTLYEDYQL TFTIPEGRWL EDMIEIISEE TNITEEEFVE
AVTDKEYIED LIERFTILEP VVLDEQIRWP LEGYLFPARY DFVEEEIDVK LLIETMLSRT
SEILLKYYND ESGFTYHEVL TIASIIEGES RNDDERALIS GIIHNRLTAN NMPLQMDPTV
AYAHGEHFSR TLYEHLEIDS PYNTYKVQGL PVGPINSPGE ASIRAALQPE QHQYLYFYHA
EDGEIYPSKT YNEHQEILQE YRDSTEE
//
