ID F3NTX3_9ACTN Unreviewed; 287 AA.
AC F3NTX3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=SGM_6423 {ECO:0000313|EMBL:EGG43283.1};
OS Streptomyces griseoaurantiacus M045.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=996637 {ECO:0000313|EMBL:EGG43283.1, ECO:0000313|Proteomes:UP000003022};
RN [1] {ECO:0000313|EMBL:EGG43283.1, ECO:0000313|Proteomes:UP000003022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M045 {ECO:0000313|EMBL:EGG43283.1,
RC ECO:0000313|Proteomes:UP000003022};
RX PubMed=21551298; DOI=10.1128/JB.05053-11;
RA Li F., Jiang P., Zheng H., Wang S., Zhao G., Qin S., Liu Z.;
RT "Draft genome sequence of the marine bacterium Streptomyces
RT griseoaurantiacus M045, which produces novel manumycin-type antibiotics
RT with a pABA core component.";
RL J. Bacteriol. 193:3417-3418(2011).
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:EGG43283.1}.
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DR EMBL; AEYX01000046; EGG43283.1; -; Genomic_DNA.
DR RefSeq; WP_006144317.1; NZ_AEYX01000046.1.
DR AlphaFoldDB; F3NTX3; -.
DR STRING; 996637.SGM_6423; -.
DR eggNOG; COG1559; Bacteria.
DR Proteomes; UP000003022; 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 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:UP000003022};
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 161
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 287 AA; 30869 MW; E5273C85D04A6D3D CRC64;
MQTHSPRRNA RSTVRLTPRG RAALVATGAV LAVAAVAVPL LTLGAGDGEH RPRRLVIPEG
RRAGQVYEAV DKALALPAGT TAKSLPKAEL KLPAEAHGNP EGYLFPATYP IDGKTTPQSL
LRSMVDTARK RFDGGGTTAG ARSGTASVYR TVTLASIVQA EADREADMGK VARVVVNRLR
RGMPLQMDST LDYALHRFSP VLSTADTKLD SPYNTYRRMG LPPTPISNPG EDALRAALHP
TPGNWLYFVT VGPGDTRFSA TYEEHRRNVA ALDLRRESRT PSSAAPR
//
