ID A0A9J6RAE3_9BACI Unreviewed; 417 AA.
AC A0A9J6RAE3;
DT 28-JUN-2023, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2023, sequence version 1.
DT 02-APR-2025, entry version 6.
DE RecName: Full=Endolytic murein transglycosylase {ECO:0000256|HAMAP-Rule:MF_02065};
DE EC=4.2.2.29 {ECO:0000256|HAMAP-Rule:MF_02065};
DE AltName: Full=Peptidoglycan lytic transglycosylase {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:MCZ0702334.1};
GN ORFNames=OWO01_03790 {ECO:0000313|EMBL:MCZ0702334.1};
OS Natronobacillus azotifigens.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Natronobacillus.
OX NCBI_TaxID=472978 {ECO:0000313|EMBL:MCZ0702334.1, ECO:0000313|Proteomes:UP001084197};
RN [1] {ECO:0000313|EMBL:MCZ0702334.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=24KS-1 {ECO:0000313|EMBL:MCZ0702334.1};
RA Sorokin D.Y., Merkel A.Y.;
RT "WGS of Natronobacillus azotifigens 24KS-1, an anaerobic diazotrophic
RT haloalkaliphile from soda-rich habitats.";
RL Submitted (NOV-2022) 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 -!- CATALYTIC ACTIVITY:
CC Reaction=a peptidoglycan chain = a peptidoglycan chain with N-
CC acetyl-1,6-anhydromuramyl-[peptide] at the reducing end + a
CC peptidoglycan chain with N-acetylglucosamine at the non-reducing
CC end.; EC=4.2.2.29; Evidence={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:MCZ0702334.1}.
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DR EMBL; JAPRAT010000005; MCZ0702334.1; -; Genomic_DNA.
DR RefSeq; WP_268779103.1; NZ_JAPRAT010000005.1.
DR Proteomes; UP001084197; 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; 3.30.160.60; 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; ENDOLYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR PANTHER; PTHR30518:SF2; ENDOLYTIC MUREIN TRANSGLYCOSYLASE; 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:UP001084197};
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 70..90
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..55
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 301
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 417 AA; 48002 MW; 91F1B44871C534FA CRC64;
MSNSEEEQHT QLSEQKNEEN QDQRIKDENT SNDKAEEIEQ EKSMEKNNRK QTREERFIQR
CKDASIVRKI VAITITVLTI LMVFGAVRIY NYVQSGLSPV DPDDQSVVEV EIPMGSSSRS
IAEILEEEGV INDALFYRLY VNINNVGSFQ AGNYELTPAM TLEEITEILQ SGTVPPLFRV
TIPEGRTIEE IAILYENGAN IDADEFLDLM RDEEYIEGLI DEFPNILSEE ILNEDIRYAL
EGYLFPATYP FYEENPTIDQ IIRDMLRRTD QVISSHFGEI AQLEQFSVHE IITFASIVER
EARDEEERMK IAGVFYNRLE EGMRLETDPT VLYALGEHRE RVMFSDLEVE SPYNTYRVHG
LPVGPISNFG ESSLRAVLDP ANTNYLFFVA APDGEIYFSE TFEEHRDLAN EHLDRDL
//
