ID A0A1H9S4L0_9LACT Unreviewed; 393 AA.
AC A0A1H9S4L0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, 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 ORFNames=SAMN04488559_10694 {ECO:0000313|EMBL:SER79921.1};
OS Isobaculum melis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Isobaculum.
OX NCBI_TaxID=142588 {ECO:0000313|EMBL:SER79921.1, ECO:0000313|Proteomes:UP000198948};
RN [1] {ECO:0000313|EMBL:SER79921.1, ECO:0000313|Proteomes:UP000198948}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13760 {ECO:0000313|EMBL:SER79921.1,
RC ECO:0000313|Proteomes:UP000198948};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 ---------------------------------------------------------------------------
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; FOHA01000006; SER79921.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9S4L0; -.
DR STRING; 142588.SAMN04488559_10694; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000198948; 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; 3.30.1490.480; 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:UP000198948};
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 40..63
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 276
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 393 AA; 44359 MW; A127C70B225E3564 CRC64;
MGKENEPSSQ KKFDWKKDWK QDATPKKLER QKESKIVRRI VFSIVASVVV VLAIVAFIGY
NYVQSALKPL DAKSTEQIQI EVPMGSSTKL IAKLLEEEKI IKDATVFSYY VKTNNTGEFQ
SGYYQLSPAM SLDEIIKELQ AGGTAEPYEV SGKILVKEGD TVDQIADTIA EHTDFTKEEF
LALMTNEAFL QQMSGRYTHL LESAMTAEGV RYRLEGYLFP ATYDYDEEKT TLEDLVASML
QKTDEILSKD NFYSEIEAQG KTTQEVLAIA SLVEKEGVTP EDRAKIASAF YNRIEQGMPL
QSDISILYAL GVHKELVTYD DLEIDSPYNL YQHTGVGPGP FGNPGEEAIR ATLHPADTNY
IYFVADIKTK IVYFAETYEE HLILKDKYVD NPE
//
