ID A0A090Q393_9FLAO Unreviewed; 346 AA.
AC A0A090Q393;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=JCM19294_65 {ECO:0000313|EMBL:GAK97529.1};
OS Nonlabens tegetincola.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Nonlabens.
OX NCBI_TaxID=323273 {ECO:0000313|EMBL:GAK97529.1, ECO:0000313|Proteomes:UP000029221};
RN [1] {ECO:0000313|EMBL:GAK97529.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 19294 {ECO:0000313|EMBL:GAK97529.1};
RA Nakanishi M., Meirelles P., Suzuki R., Takatani N., Mino S., Suda W.,
RA Oshima K., Hattori M., Ohkuma M., Hosokawa M., Miyashita K., Thompson F.L.,
RA Niwa A., Sawabe T., Sawabe T.;
RT "Draft Genome Sequences of Marine Flavobacterium Nonlabens Strains NR17,
RT NR24, NR27, NR32, NR33, and Ara13.";
RL Genome Announc. 2:e01165-14(2014).
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:GAK97529.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BBML01000006; GAK97529.1; -; Genomic_DNA.
DR RefSeq; WP_042279198.1; NZ_BBML01000006.1.
DR AlphaFoldDB; A0A090Q393; -.
DR STRING; 319236.BST91_05860; -.
DR eggNOG; COG1559; Bacteria.
DR Proteomes; UP000029221; 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:UP000029221};
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 217
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 346 AA; 39721 MW; E9739FE94416DB9C CRC64;
MNKYRKIILG VVLVGLLFMA GFAYKVYTTF LSPNTNFESE TYEVFIPSDA DYNKAFLIFA
DAVEDRDALH QTAVRKKYHE NVKAGRFLIK KGSSNNDIIN TLRSGNTPVK VRFNNQERIE
DLAGRLAAQV EPDSLSLLKA FTDSTFLNQA GVSREEALTL FLPNTYDSYW NTTATSLRDK
LYSYHQQYWN ENRRSLASKQ RLSPSQAYIL ASIVHKETAM KDERARVAGV YLNRLKKNIK
LDADPTVIYA KKKKDGDFNQ VIKQVLYKHL EIDSEYNTYK NAGLPPGPIV TPDIDAINAV
LQPENHDYFY FVADVQNFGY HKFAKTLTQH NINAAAYRRW IKRNNK
//
