ID A0A1I5W803_9ACTN Unreviewed; 386 AA.
AC A0A1I5W803;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=SAMN04489713_12332 {ECO:0000313|EMBL:SFQ15791.1};
OS Actinomadura madurae.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=1993 {ECO:0000313|EMBL:SFQ15791.1, ECO:0000313|Proteomes:UP000183413};
RN [1] {ECO:0000313|EMBL:SFQ15791.1, ECO:0000313|Proteomes:UP000183413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43067 {ECO:0000313|EMBL:SFQ15791.1,
RC ECO:0000313|Proteomes:UP000183413};
RA de Groot N.N.;
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; FOVH01000023; SFQ15791.1; -; Genomic_DNA.
DR RefSeq; WP_024935462.1; NZ_FOVH01000023.1.
DR AlphaFoldDB; A0A1I5W803; -.
DR STRING; 1993.SAMN04489713_12332; -.
DR eggNOG; COG1559; Bacteria.
DR InParanoid; A0A1I5W803; -.
DR Proteomes; UP000183413; 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:UP000183413};
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 42..66
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 263
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 386 AA; 42263 MW; E4CAB1724D8D09FA CRC64;
MNDLDLFSDP YGDGPPPGER PGRREQRRVR KKQKRRRRNG RAAALFAMAF LVAVFGTGGV
LGYAWLDNKW HPPDYDGQGA GNVTVQIKDG ASGSVIGATL EEHRVVKSSR AFVKAYNKET
KASSIQPGFY QMRLRMSSSA AMALLLDPKS RAGNQITIPE GRRAIEVFEL LAKKTGISVK
EFQAAAKKPQ GLGLPAYAKG KVEGYLYPGR YDLDPNGTAA QILKQMVGRF NQEASSVDLV
GKAREAKMSP ATVITLASLI QAEGGKPSDL PKISRVIYNR VARGMPLQFD TTVLYALNKR
TLTVTNEDLK VDSPYNTYTN KGLPPGPIAN PGPDAIEAAL APKDGTWLYF IATDPTNKIT
KFATTEPERQ AIEKEFRAWQ RAHPGQ
//
