ID C0M807_STRE4 Unreviewed; 524 AA.
AC C0M807;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 80.
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 OrderedLocusNames=SEQ_1880 {ECO:0000313|EMBL:CAW95061.1};
OS Streptococcus equi subsp. equi (strain 4047).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=553482 {ECO:0000313|EMBL:CAW95061.1, ECO:0000313|Proteomes:UP000001365};
RN [1] {ECO:0000313|EMBL:CAW95061.1, ECO:0000313|Proteomes:UP000001365}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4047 {ECO:0000313|EMBL:CAW95061.1,
RC ECO:0000313|Proteomes:UP000001365};
RX PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F.,
RA Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M.,
RA Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A.,
RA Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C.,
RA Maskell D.J., Parkhill J., Waller A.S.;
RT "Genomic evidence for the evolution of Streptococcus equi: host
RT restriction, increased virulence, and genetic exchange with human
RT pathogens.";
RL PLoS Pathog. 5:E1000346-E1000346(2009).
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; FM204883; CAW95061.1; -; Genomic_DNA.
DR RefSeq; WP_012680062.1; NC_012471.1.
DR AlphaFoldDB; C0M807; -.
DR KEGG; seu:SEQ_1880; -.
DR HOGENOM; CLU_025574_1_0_9; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000001365; 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; 3.30.160.60; Classic Zinc Finger; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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 157..181
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 64..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 20..54
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 67..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 401
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 524 AA; 57695 MW; 3FE8E40980037156 CRC64;
MALTDFKDDE QRRQQQKSFK EKILAELEKA NQIRKEKEEE LFKKDLEVQE AARRTAQLYA
EYKRQEALSN NPKQASDIAA ASQETTSTAS TAHTSAIKLE ETAVATGDQA LSPPEEPALS
ESLLKEEASV EGQTKKGGPV RRKTSKRQQT DRMAKKISTV LISSIVAIIV VIGLAGTAYV
YSALNPVDKN SDDFVQVEIP AGSGNKLIGQ ILEKEGLIKN STVFSFYTKF KNFTNFQSGY
YNLQKSMSLE DIAQALQEGG TAEPTKPVLG KILIPEGYTI KQIAKAIETN SRAKNRSKAK
TPFHSKDFLN LVTSDAFIQE MAKKYPKLLG DLPSKEVATY QLEGYLFPAT YNYYKETTLK
DLAEEMIAAA NANLAPYYEA IAASGKTVNE VLTLASLVEK EGSTDDDRRQ IASVFYNRLN
NGMALQSNIA ILYAMGKLGE KTTLAEDAAI DTTINSPYNV YINTGLMPGP VDSPGLAAIE
ATINPAATDY VYFVADVRTG EVYYAKTFEE HSANVEKYVN SQIQ
//
