ID A0A926TZ67_9CYAN Unreviewed; 358 AA.
AC A0A926TZ67;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 05-FEB-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:MBD2090311.1};
GN ORFNames=H6F67_10645 {ECO:0000313|EMBL:MBD2090311.1};
OS Microcoleus sp. FACHB-1515.
OC Bacteria; Bacillati; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Microcoleus.
OX NCBI_TaxID=2692821 {ECO:0000313|EMBL:MBD2090311.1, ECO:0000313|Proteomes:UP000646638};
RN [1] {ECO:0000313|EMBL:MBD2090311.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FACHB-1515 {ECO:0000313|EMBL:MBD2090311.1};
RX PubMed=32943748;
RA Chen M.Y., Teng W.K., Zhao L., Hu C.X., Zhou Y.K., Han B.P., Song L.R.,
RA Shu W.S.;
RT "Comparative genomics reveals insights into cyanobacterial evolution and
RT habitat adaptation.";
RL ISME J. 0:0-0(2020).
RN [2] {ECO:0000313|EMBL:MBD2090311.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FACHB-1515 {ECO:0000313|EMBL:MBD2090311.1};
RA Chen M., Teng W., Zhao L., Hu C., Zhou Y., Han B., Song L., Shu W.;
RL Submitted (AUG-2020) 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:MBD2090311.1}.
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DR EMBL; JACJPO010000030; MBD2090311.1; -; Genomic_DNA.
DR Proteomes; UP000646638; 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:UP000646638};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 230
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 358 AA; 40002 MW; 600E3750ADAB5206 CRC64;
MTIARRISKG FFYLLVFPAT LGVCAWQGWS WWSWATAPAR AGEAADSTVQ IEIPPGTSAQ
QIGADLESAG LIRSRRAWNL WTRWQGLQNR EGGFQAGTYE LSPASPLDEI ANQVWQGDVV
QASFTIPEGW SMRQMAAYFE EEGFFSADAF LAAARQVPYD RYPWLPKDLP HLEGFLFPDT
YQTPENPTPE QVVNQMLDRF EQVALPVYQE GQSDYSLKDW VTLSSIVEKE SVVDEERDTI
ASVFARRLRE SIPLGADPTV EYAFNLRQAP GQPLTLAQVR QPSPYNTYIN AGLPPTPIAS
PGLASLEASL KPQDTEYLYF VARYDGTHVF SRTLAEHEAA QIKIQDDLAA QPSESTPN
//
