ID A0A0D6MJH4_9PROT Unreviewed; 329 AA.
AC A0A0D6MJH4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, 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=Tasa_010_309 {ECO:0000313|EMBL:GAN53762.1};
OS Tanticharoenia sakaeratensis NBRC 103193.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Tanticharoenia.
OX NCBI_TaxID=1231623 {ECO:0000313|EMBL:GAN53762.1, ECO:0000313|Proteomes:UP000032679};
RN [1] {ECO:0000313|EMBL:GAN53762.1, ECO:0000313|Proteomes:UP000032679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 103193 {ECO:0000313|EMBL:GAN53762.1,
RC ECO:0000313|Proteomes:UP000032679};
RA Azuma Y., Hadano H., Hirakawa H., Matsushita K.;
RT "Genome sequencing of Tanticharoenia sakaeratensis NBRC 103193.";
RL Submitted (OCT-2012) 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 -!- 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:GAN53762.1}.
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DR EMBL; BALE01000010; GAN53762.1; -; Genomic_DNA.
DR RefSeq; WP_048847939.1; NZ_BAQF01000003.1.
DR AlphaFoldDB; A0A0D6MJH4; -.
DR STRING; 1231623.Tasa_010_309; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000032679; 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 inner membrane {ECO:0000256|HAMAP-Rule:MF_02065};
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:UP000032679};
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 200
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 329 AA; 34600 MW; D0C0299EFFD7A962 CRC64;
MRALAVLLCV LLGAGGAWLG ARYLYDAPGP LPATRDVLVH HGDSAVVAAS LQRGGVVQPG
RWGRLAFQVA ARLTRGDGAL HAAEFAFPAH ASLRETLSIL RHAHPVQHPL TVPEGLTAMQ
IASLLRAAPF LAGDVPAIAE GSVLPQTISY EYGTSRAKLV ARLQGMMTVA LAKVWAEREP
DPSVPDPQAL LTLASMVERE TATAAERPLV ARVFLNRLRD HMRLQSDPTV IYAVTHGAQT
GGTLADDAGG RAALTHADLS FVSPYNTYTV EGLPPGPICS PGLASLEAAA HPARSDAEYF
VANGSGATSF ATTLDAHNRN VALRRQGGK
//
