ID A0A3M2JGF9_9CELL Unreviewed; 388 AA.
AC A0A3M2JGF9;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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 ECO:0000313|EMBL:RMI13107.1};
GN ORFNames=EBM89_05935 {ECO:0000313|EMBL:RMI13107.1};
OS Cellulomonas triticagri.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=2483352 {ECO:0000313|EMBL:RMI13107.1, ECO:0000313|Proteomes:UP000269289};
RN [1] {ECO:0000313|EMBL:RMI13107.1, ECO:0000313|Proteomes:UP000269289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEAU-YY56 {ECO:0000313|EMBL:RMI13107.1,
RC ECO:0000313|Proteomes:UP000269289};
RA Han C.;
RT "Isolation, diversity and antifungal activity of actinobacteria from
RT wheat.";
RL Submitted (OCT-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:RMI13107.1}.
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DR EMBL; RFFI01000022; RMI13107.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M2JGF9; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000269289; 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 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:UP000269289};
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 43..64
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 263
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 388 AA; 41447 MW; 0E5B88689F17B7FC CRC64;
MSDLFLGAPQ QEHHEAPPPS RRSRRDDKAI KARRRKTRRR RSASVLVLAL ALVGGMAFVV
WSIFGGLFSG GGGGDDSVSD FPGPGSGEVQ VTVASGDTGG AIGATLEEAG VVATAKAFTD
AYAANPAATG IQPGAYTLLM EMKASDAVNA LLDAENRVSN RVTIPEGYTA DQIYQRLYEI
TTIPVEDFEA AAADPAAIGL PAEAGGNVEG WLFPATYDVE PGSTAASVLS QMVARTVSIL
TDRGVAQDQW ETVLNKASIV EREGKLDEDR AKIARAIQNR LDIEMALQID AINAYGLGIP
GTQLTTADTR DAQPPYNPYN SYKIPGLPPT PIANPGEVSI DAVLNPADGP WLFWVTVNLD
TGETKFSETF AEHQTYVDEL RAWQRENQ
//
