MLTG_HAEIN
ID MLTG_HAEIN Reviewed; 347 AA.
AC P44720;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Endolytic murein transglycosylase {ECO:0000255|HAMAP-Rule:MF_02065};
DE EC=4.2.2.- {ECO:0000255|HAMAP-Rule:MF_02065};
DE AltName: Full=Peptidoglycan polymerization terminase {ECO:0000255|HAMAP-Rule:MF_02065};
GN Name=mltG {ECO:0000255|HAMAP-Rule:MF_02065}; OrderedLocusNames=HI_0457;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Functions as a peptidoglycan terminase that cleaves nascent
CC peptidoglycan strands endolytically to terminate their elongation.
CC {ECO:0000255|HAMAP-Rule:MF_02065}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02065}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_02065}.
CC -!- SIMILARITY: Belongs to the transglycosylase MltG family.
CC {ECO:0000255|HAMAP-Rule:MF_02065}.
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DR EMBL; L42023; AAC22115.1; -; Genomic_DNA.
DR PIR; E64069; E64069.
DR RefSeq; NP_438618.1; NC_000907.1.
DR RefSeq; WP_005693707.1; NC_000907.1.
DR AlphaFoldDB; P44720; -.
DR SMR; P44720; -.
DR STRING; 71421.HI_0457; -.
DR PRIDE; P44720; -.
DR EnsemblBacteria; AAC22115; AAC22115; HI_0457.
DR KEGG; hin:HI_0457; -.
DR PATRIC; fig|71421.8.peg.477; -.
DR eggNOG; COG1559; Bacteria.
DR HOGENOM; CLU_025574_0_2_6; -.
DR OMA; IAMPGKA; -.
DR PhylomeDB; P44720; -.
DR BioCyc; HINF71421:G1GJ1-473-MON; -.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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 HAMAP; MF_02065; MltG; 1.
DR InterPro; IPR003770; MLTG-like.
DR PANTHER; PTHR30518; PTHR30518; 1.
DR Pfam; PF02618; YceG; 1.
DR TIGRFAMs; TIGR00247; TIGR00247; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cell wall biogenesis/degradation;
KW Lyase; Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..347
FT /note="Endolytic murein transglycosylase"
FT /id="PRO_0000168818"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02065"
FT SITE 224
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02065"
SQ SEQUENCE 347 AA; 39621 MW; A21D559C66308F3D CRC64;
MKKFLIAILL LILILAGVAS FSYYKMTEFV KTPVNVQADE LLTIERGTTS SKLATLFEQE
KLIADGKLLP YLLKLKPELN KIKAGTYSLE NVKTVQDLLD LLNSGKEVQF NVKWIEGKTF
KDWRKDLENA PHLVQTLKDK SNEEIFALLD LPDIGQNLEL KNVEGWLYPD TYNYTPKSTD
LELLKRSAER MKKALNKAWN ERDEDLPLAN PYEMLILASI VEKETGIANE RAKVASVFIN
RLKAKMKLQT DPTVIYGMGE NYNGNIRKKD LETKTPYNTY VIDGLPPTPI AMPSESSLQA
VANPEKTDFY YFVADGSGGH KFTRNLNEHN KAVQEYLRWY RSQKNAK