ID A0A0B5F7L9_STRA4 Unreviewed; 667 AA.
AC A0A0B5F7L9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 29.
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=SLNWT_6440 {ECO:0000313|EMBL:AJE86816.1};
OS Streptomyces albus (strain ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 /
OS NBRC 107858).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1081613 {ECO:0000313|EMBL:AJE86816.1, ECO:0000313|Proteomes:UP000031523};
RN [1] {ECO:0000313|EMBL:AJE86816.1, ECO:0000313|Proteomes:UP000031523}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 21838 / DSM 41398 / FERM P-419 / JCM 4703 / NBRC 107858
RC {ECO:0000313|Proteomes:UP000031523};
RA Lu C.;
RT "Enhanced salinomycin production by adjusting the supply of polyketide
RT extender units in Streptomyce albus DSM 41398.";
RL Submitted (JAN-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 -!- SIMILARITY: Belongs to the transglycosylase MltG family.
CC {ECO:0000256|HAMAP-Rule:MF_02065}.
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DR EMBL; CP010519; AJE86816.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B5F7L9; -.
DR KEGG; sals:SLNWT_6440; -.
DR Proteomes; UP000031523; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
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:UP000031523};
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 REGION 1..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..47
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 540
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 667 AA; 71584 MW; AA58E8CAC40B9CC8 CRC64;
MTEYGRGPGP DPWHPDDPLY GDGYRGQQAE GQGPAYGDQS PQQYESWQHG APDPAYGQGP
YASGDPYGTG QYQQPYDTGT HGTHEGYGQQ QYGTGQQPYD TGRHPQQSYD TGPQQPYDTG
QHPQQPYGPG HYDTGQQSYG GGDPSYGGQQ SYGTGQYESG WDGGAQAQGG QGGYGSGVPV
DPYGGQDPYG GRDPRGGQDP YGGQGGHPHG GAPGDHYGDP AGQGQQARPQ GAAPQEPGQG
RRRPPQPEAA ARAGADDPGS GWDPGPDQGE HAFFAGGDQD DDDFDEGRAG RRGRSARRGG
GGGGGKKSRS GLSCMVATVL LAGVIGGGGY FGYQFYQDRF GPAPDYSGEG SGTVSVEIPA
GASGYDIGQA LKKKGIVKSV QAFVDAQGDN PDGQRIQHGF YTLREQMSGK SAVTLMLDPK
SRNALIIGEG RRNTQIYAEI DKRLGIASGT TQKVAKKEWR SLGLPKWAEN GSKRKDPLEG
FLYPASYPVD KSMKPADVLE RMVKRADSEY AKYDLAGKAE ELDLKDPLQL VTVASLVQAE
GITHEDFRRM AAVVYNRLKP SNTVTNQKLE FDSTYNYLKN KSNIDIPTSE IRSYDDPYNT
YFYRGLTPGP IGNPGEDALK AAIGPDSGGW MFFISIDCKT TTFSKTLKEH EKYVAEFNKA
RKEGKCE
//
