ID A0A1W7D492_9ACTN Unreviewed; 600 AA.
AC A0A1W7D492;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=CAG99_25505 {ECO:0000313|EMBL:ARQ71739.1};
OS Streptomyces marincola.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2878388 {ECO:0000313|EMBL:ARQ71739.1, ECO:0000313|Proteomes:UP000194218};
RN [1] {ECO:0000313|EMBL:ARQ71739.1, ECO:0000313|Proteomes:UP000194218}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCSIO 03032 {ECO:0000313|EMBL:ARQ71739.1,
RC ECO:0000313|Proteomes:UP000194218};
RA Ma L., Zhu Y., Zhang W., Zhang G., Tian X., Zhang S., Zhang C.;
RT "Complete genome sequence of Streptomyces sp. SCSIO 03032 revealed the
RT diverse biosynthetic pathways for its bioactive secondary metabolites.";
RL Submitted (MAY-2017) 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; CP021121; ARQ71739.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W7D492; -.
DR KEGG; smao:CAG99_25505; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000194218; Chromosome.
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:UP000194218};
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 261..281
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 1..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..247
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 475
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 600 AA; 64923 MW; 14060DF46B7B684F CRC64;
MTDDGRNPGS EPWYPDDPRY ADQGWSGGYE GAGGQPAQQG SWQHHYGAQQ QYHGQQYDAQ
PGYDAQQYGG QQYGDGRPYA ANDPRYGDGQ QYHPQQPYQE QGGWDTAGGH YGQGYGHDPY
ATAGQPGPVQ DPGGYQGGYG ADQGYPGQPY DTAAHQPGQD GHPYASDQQY ARQPGHPGAA
PQPEHERQQA PGAAGGQPGE RRREPEPDPE TGWDPGPDQG ELDFFRRDDD EDEGRPGDSG
RGSGRRGDRQ KSAKRRRGSR GCAVAAVLVL AGVGGVGYYG YDFYQERFGP APDYQGEGTG
EVQVTIPDGA TVSQMANILR EAGVVRSHDA FVDAAGGQAL QAGVYTLREQ MSAESAVAMM
LNGEAVGGLI VPEGRRATEV YTMIDEYLGL PEGATAEAAE AADLGLPDWA EGDPEGFLFP
ARYDVGTDTA PEEVLRQMVQ RATAEFTETD LETQAASIGR TPREVLVIAS LIEAEGQSDE
EFVRVSRVIH NRLEQNIRLE FDSTVNYALG RHTLDVSLDD TDIDSPYNTY EEFGLPPGPI
ANPGHAAIEA ALNPADGPWL FFVTVRPGDT RFTDDYDEHL QNVLDFNAVQ QENREQEGGG
//
