ID A0A0Q9P0B9_9MICC Unreviewed; 562 AA.
AC A0A0Q9P0B9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=ASG77_01560 {ECO:0000313|EMBL:KRE80675.1};
OS Arthrobacter sp. Soil762.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1736401 {ECO:0000313|EMBL:KRE80675.1, ECO:0000313|Proteomes:UP000051715};
RN [1] {ECO:0000313|Proteomes:UP000051715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil762 {ECO:0000313|Proteomes:UP000051715};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE80675.1, ECO:0000313|Proteomes:UP000051715}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil762 {ECO:0000313|EMBL:KRE80675.1,
RC ECO:0000313|Proteomes:UP000051715};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KRE80675.1}.
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DR EMBL; LMSG01000001; KRE80675.1; -; Genomic_DNA.
DR RefSeq; WP_056340281.1; NZ_LMSG01000001.1.
DR AlphaFoldDB; A0A0Q9P0B9; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000051715; 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 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 220..241
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 1..194
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 COMPBIAS 20..34
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..77
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 433
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 562 AA; 59697 MW; 56E8DA1CDFCACD30 CRC64;
MSPSNNDDTS GATSNDGARP LTRKELRALE KHTGSSDVVP EQAYETGHDA PAPATAPVPE
AAPAPGPAAV PEPQPEPVHA HEPVHVPEPA PEPEPAIPTA PDTPPSIQHA GPAADHHPDD
AQVQEHHPED QHFNEAHDAG HHHFPDEAHD AGHHYPDEAH HDAGHHYPGQ AVHDAGHLDD
HHVDDHDPDD HHAASGLFAG AAAGSVVTKP SKKVRRRRRL LALFLTLVVF VAAIAVGAQF
LKPLLGNDKA ADYPGPGTGE VIVSVQPGEG TRSVATKLES GKVVANADTF LQAFASSGGT
LSPGDYTFKT EMKNSDAVSI LLGTDKSKVI YFALNAGLRI GESLQAISEG SGVSLQQLKE
LSNAPAQFGL PANAKNLEGF LAPGEYRFPL GTPAKEILQS LVKGTTDELV AQGISDPAKQ
YEAVIVASIV QAEGGQAEYG DVAGAIYNRL KPNDQTYGYL QVDSAVTYGL GTKSFNFTDE
ERQDKSNLYN TYANPGLPPG PIGSPGKTAI DAAAKPKTND YLYWVTINLD TKETKFSKTL
DEHNVYVNEY NTWCQANVGR CT
//
