ID A0A0M4HA35_9GAMM Unreviewed; 349 AA.
AC A0A0M4HA35;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-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=AMQ28_02980 {ECO:0000313|EMBL:ALD01409.1};
OS Acinetobacter sp. TTH0-4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1646498 {ECO:0000313|EMBL:ALD01409.1, ECO:0000313|Proteomes:UP000055186};
RN [1] {ECO:0000313|EMBL:ALD01409.1, ECO:0000313|Proteomes:UP000055186}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TTH0-4 {ECO:0000313|EMBL:ALD01409.1,
RC ECO:0000313|Proteomes:UP000055186};
RA Zhang G.;
RT "Acinetobacter qinghaiensis sp. nov., isolated from active layer of
RT permafrost region.";
RL Submitted (SEP-2015) 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 inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_02065}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_02065}.
CC -!- SIMILARITY: Belongs to the transglycosylase MltG family.
CC {ECO:0000256|HAMAP-Rule:MF_02065}.
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DR EMBL; CP012608; ALD01409.1; -; Genomic_DNA.
DR RefSeq; WP_053578295.1; NZ_CP012608.1.
DR AlphaFoldDB; A0A0M4HA35; -.
DR STRING; 1646498.AMQ28_02980; -.
DR KEGG; att:AMQ28_02980; -.
DR PATRIC; fig|1646498.3.peg.613; -.
DR Proteomes; UP000055186; Chromosome.
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; 3.30.160.60; Classic Zinc Finger; 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 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 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 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 228
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 349 AA; 39352 MW; B6B801168A32C4E5 CRC64;
MPTTKQKSKK KATKILPLKG LGLLMLGFIG LAFVILWSSL FKAYPVKGQK QMLAIGTGDT
YSGFIDRLGE EDKVSFPIIL KLYQKFIIHD TLKAGVYEVQ KGMSIRQVME MLSNSENAQM
NRILVIEGTT FKQLLEQLKK DDLVTKDVLN LPQEQMLKAL NIPFEHPEGL FAPDTYFFAK
GETDKKILTD LYQRQMKSLD KAWEKRATDL PYKNKYEALI MASIIEKETS LDRELEQVSG
VFVRRLKLGM RLQTDPTVIY GMGENYTGNI TRADLRTPTA YNTYTNNGLP PTPIALPSQK
AIEAAMHPDN AKNIYFVATG NGGHTFTASL DEHNRAVQDY LAVLKAKKD
//
