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Database: UniProt
Entry: S9TV45_PAEAL
LinkDB: S9TV45_PAEAL
Original site: S9TV45_PAEAL 
ID   S9TV45_PAEAL            Unreviewed;       353 AA.
AC   S9TV45;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=PAALTS15_16696 {ECO:0000313|EMBL:EPY06136.1};
OS   Paenibacillus alvei TS-15.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1117108 {ECO:0000313|EMBL:EPY06136.1, ECO:0000313|Proteomes:UP000015344};
RN   [1] {ECO:0000313|EMBL:EPY06136.1, ECO:0000313|Proteomes:UP000015344}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TS-15 {ECO:0000313|EMBL:EPY06136.1,
RC   ECO:0000313|Proteomes:UP000015344};
RA   Strain E.A., Brown E., Allard M.W., Luo Y.L.;
RL   Submitted (MAY-2013) 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}.
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:EPY06136.1}.
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DR   EMBL; ATMT01000057; EPY06136.1; -; Genomic_DNA.
DR   RefSeq; WP_021260646.1; NZ_ATMT01000057.1.
DR   AlphaFoldDB; S9TV45; -.
DR   PATRIC; fig|1117108.3.peg.3445; -.
DR   eggNOG; COG1559; Bacteria.
DR   Proteomes; UP000015344; Unassembled WGS sequence.
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   CDD; cd08010; MltG_like; 1.
DR   Gene3D; 3.30.160.60; Classic Zinc Finger; 1.
DR   Gene3D; 3.30.1490.480; Endolytic murein transglycosylase; 2.
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   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   SITE            234
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ   SEQUENCE   353 AA;  39516 MW;  690AB7B3EEAB7B25 CRC64;
     MKKGSKVLLT ISFVLLLVAG ASVGYIWSGM RPLAQEEREI PVSIQQGSGT AAIASQLEEQ
     GIIRNALIFK VYLKWNGEGS RFQAGKYAFR PGVTYDDIIA KLNSGEVVPE EMVRFTIPEG
     YTVEQIADKL SNDGIVDKDQ FLKLANDTAW LKGQAPIAEH IPTDAKLKHR LEGYLFPETY
     ELKKGSSEEE IIARMVQETE KRLPQASATW ESDLKTRGLT LHDMLTLASL VEREAVVDAE
     RPLIAGVIDN RIAKGMRLQI DATVQYALDK PKERLYYKDL EIDSPYNTYK IDKLPPGPIS
     SPSTASIQAV LKPEASEYLY YVTKKDGTHT HLFAKTFPEH QRNIEQSKKM AAQ
//
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