ID A0A0Q2XU11_9RHOB Unreviewed; 386 AA.
AC A0A0Q2XU11;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=AN189_04425 {ECO:0000313|EMBL:KQI69646.1};
OS Loktanella sp. 3ANDIMAR09.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Loktanella.
OX NCBI_TaxID=1225657 {ECO:0000313|EMBL:KQI69646.1, ECO:0000313|Proteomes:UP000051463};
RN [1] {ECO:0000313|EMBL:KQI69646.1, ECO:0000313|Proteomes:UP000051463}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3ANDIMAR09 {ECO:0000313|EMBL:KQI69646.1,
RC ECO:0000313|Proteomes:UP000051463};
RA Mas-Llado M., Nogales B., Bosch R.;
RT "Draft genome sequence of Loktanella sp. 3ANDIMAR09.";
RL Submitted (SEP-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}.
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:KQI69646.1}.
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DR EMBL; LJAK01000002; KQI69646.1; -; Genomic_DNA.
DR RefSeq; WP_056031622.1; NZ_LJAK01000002.1.
DR AlphaFoldDB; A0A0Q2XU11; -.
DR STRING; 1225657.AN189_04425; -.
DR PATRIC; fig|1225657.3.peg.905; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000051463; 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; 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 inner membrane {ECO:0000256|HAMAP-Rule:MF_02065};
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:UP000051463};
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 259
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 386 AA; 41323 MW; 5315D2DF393A50BA CRC64;
MWRHIASNAL TFMVVALFVS AGVVAWGTQQ YSNPGPLAQG ICLQVPGGSN MRRVSEDLEA
QGAVSSAAIF RMGADYTEKA SELKAGSFLI AEGASMAEIV DTVTRGGAST CGTEIVYRVG
VRVNEVQVRE LDPATGRYEE VAAFTPGEGE VPSEYTAVLD AADTRLRLAV AEGTTAWQVV
QALNAIDVLE GPLDDIPAEG SLAPDSYEFT AGITRGSIID RMTERQENIL AEAWAARVDG
LPLDSPEEAL ILASLIEKET AVADERRQVA SVFVNRLERG MRLQTDPAVI YGVTEGRSVL
DRGLRRSELD TPTPWNTYTI PALPPTPIAN PGRASIEAAL DPDTTDYVFF VADGTGGHAF
ATNLDDHNRN VAAWRVIEAE RAANDG
//
