ID A0A2P8GZV2_9MICO Unreviewed; 478 AA.
AC A0A2P8GZV2;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=CLV49_3110 {ECO:0000313|EMBL:PSL39470.1};
OS Labedella gwakjiensis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Labedella.
OX NCBI_TaxID=390269 {ECO:0000313|EMBL:PSL39470.1, ECO:0000313|Proteomes:UP000241203};
RN [1] {ECO:0000313|EMBL:PSL39470.1, ECO:0000313|Proteomes:UP000241203}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21548 {ECO:0000313|EMBL:PSL39470.1,
RC ECO:0000313|Proteomes:UP000241203};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (MAR-2018) 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}.
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:PSL39470.1}.
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DR EMBL; PYAU01000001; PSL39470.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P8GZV2; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000241203; Unassembled WGS sequence.
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:UP000241203};
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 130..151
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 1..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..125
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 351
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 478 AA; 50914 MW; 59FB1C496B8F78ED CRC64;
MSRTPDKDAP SEEQDPFTAL LNGSHSADGA SRSVGPGGDP ARGATTPQPL SRREARQRSA
AERPDDTARG GSDGSPVSVP DESAETERPH ILLGTATAEQ PTVAADRASR RAAAQDDGYP
PREKRSRRGL IGTIIALLVV VGLVASGLYV WNTFEPQIRA VMGWEEPNDF EGSGTGEVLV
TIADGETGSD ISDTLASSGV TKTAEAFYKL LLAQDEDVVF QPGVYRLAKE MSAQSALDAL
QDPANKIERT AVIREGLTGA TIIEELSAAT DIPVEDFEAA IEDPTQYGVP ENAVSMEGWL
FPATYTFDPG LTATQVVKTL VDRTISSLDS AGVPVEDRER VLTIASIIQR EARQADDFYK
VSRVIQNRLD DGMRLEMDST AQYGVNEASG SVWSSAEALG SDNPWNTYQR DGLPVGPIAS
PGDVAIDAAM HPADGSWIFF VTVNLDTGET VFSNTIAEHD AAVAQLRAWC ADNPDSGC
//
