ID A0A022LIL3_9ACTN Unreviewed; 390 AA.
AC A0A022LIL3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
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=H483_0106850 {ECO:0000313|EMBL:EYT63640.1};
OS Dietzia sp. UCD-THP.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Dietziaceae;
OC Dietzia.
OX NCBI_TaxID=1292020 {ECO:0000313|EMBL:EYT63640.1, ECO:0000313|Proteomes:UP000019757};
RN [1] {ECO:0000313|EMBL:EYT63640.1, ECO:0000313|Proteomes:UP000019757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-THP {ECO:0000313|EMBL:EYT63640.1,
RC ECO:0000313|Proteomes:UP000019757};
RX PubMed=23661480;
RA Diep A.L., Lang J.M., Darling A.E., Eisen J.A., Coil D.A.;
RT "Draft Genome Sequence of Dietzia sp. Strain UCD-THP (Phylum
RT Actinobacteria).";
RL Genome Announc. 1:E00197-E00113(2013).
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 -!- 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:EYT63640.1}.
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DR EMBL; AOSR01000023; EYT63640.1; -; Genomic_DNA.
DR RefSeq; WP_017836859.1; NZ_KB714650.1.
DR AlphaFoldDB; A0A022LIL3; -.
DR eggNOG; COG1559; Bacteria.
DR HOGENOM; CLU_025574_4_1_11; -.
DR Proteomes; UP000019757; 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 Gene3D; 3.30.1490.480; Endolytic murein transglycosylase; 1.
DR HAMAP; MF_02065; MltG; 1.
DR InterPro; IPR003770; MLTG-like.
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 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..34
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 269
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 390 AA; 41501 MW; 4FEE73A03F03DAB4 CRC64;
MSAARARSRT SGTIRFILLA AVVGVVLAFA AMVYRATSSE VSAAPDFEGG GVGTALLHVE
PGDTLGVVGD RLYDIGTVAS TRAFIGAASG TSVEGIQPGY YQVRQEMSAA SAVEALSDPR
SRVGYMDVNP GGRLLDTVVV GGGTEKGIFT LIADATCLRD LDQPDAPPMC RLPQEIVDAA
VQADPAELGV PDWAINEVRG APDPVRRLEG LIAPGVHNIN PQAEPVEILR QLIDSSTEAY
DATGLVPSAE RIGLTPYQVV TAASLVEKEG TLEDFDKIAR VILNRLDEPM RLQFDSTVNY
ALADQEIATT DADRAAVTPW NTYAMDGLPY GPIGSPGLDA LRAMENPAEG QWKYFVTVDM
QGTTRFADEY PEHERYQSEA IANGVLSSGR
//
