ID A0A0N0NDL3_9ACTN Unreviewed; 589 AA.
AC A0A0N0NDL3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=OV320_3577 {ECO:0000313|EMBL:KPI30161.1};
OS Actinobacteria bacterium OV320.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592329 {ECO:0000313|EMBL:KPI30161.1, ECO:0000313|Proteomes:UP000037870};
RN [1] {ECO:0000313|EMBL:KPI30161.1, ECO:0000313|Proteomes:UP000037870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV320 {ECO:0000313|EMBL:KPI30161.1,
RC ECO:0000313|Proteomes:UP000037870};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (AUG-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:KPI30161.1}.
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DR EMBL; LJCX01000023; KPI30161.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N0NDL3; -.
DR PATRIC; fig|1592329.3.peg.2786; -.
DR Proteomes; UP000037870; 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:UP000037870};
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 235..257
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 1..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..191
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 465
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 589 AA; 64226 MW; 68E4F2CD13C972E5 CRC64;
MTEYGRGPGS EPWHPEDPLY GDGGWEGQEA PTGHQPAYGG QPQHHHYPQQ PQQQEYGDWG
QGQAQQYDQQ HYDQQQYGQQ QYDPQYQGYD QQQYGAQDQQ YTHQNQQAYH EGYQEGGWDG
TGTHAHVPFA ADPGDPYGQQ AAAYGAEQPD FYGTPEAYPP PEPPARRRAE PEPDPVPESD
AEQKTDWDPG PDQGEHAFFA GGGAEDDEDD DDPEGRGDRR GRGGKGAKSK KSRSGCACLV
VVLVFGGGVA GVGYFGYDYY KNRYAAAPDY TGDGTKQTVS IEVPKGSGGA AIGRLLKDAG
VVKSVDAFVS AVTNNPEAGG IQAGAYILKK EMSAKSAVEM MLDPASQANV MVTPGQRNVS
VYKNIDTKLG LASGTTRKLA ETEYKTLGLP AWANDNEDIK DPLEGFLFPG TYGAAKGMKP
EAVLKSMVAH ANEVYGEYDL EAKAKTLKLE SPLQVITVAS LVQAEGKTHD DYRKMAEVVY
NRLKPTNDQT NQLLQFDSTF NYLKGESKIN ISESEINSNK DPYNTYTNKG LTPGPIGNPG
EDALKATMKP TSDGWIYFVA TDGESNTEFA KTYAEFQRLK DKFDASTGN
//
