ID H6RVH3_BLASD Unreviewed; 580 AA.
AC H6RVH3;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
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 OrderedLocusNames=BLASA_2344 {ECO:0000313|EMBL:CCG03248.1};
OS Blastococcus saxobsidens (strain DD2).
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=1146883 {ECO:0000313|EMBL:CCG03248.1, ECO:0000313|Proteomes:UP000007517};
RN [1] {ECO:0000313|EMBL:CCG03248.1, ECO:0000313|Proteomes:UP000007517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD2 {ECO:0000313|EMBL:CCG03248.1,
RC ECO:0000313|Proteomes:UP000007517};
RX PubMed=22535935; DOI=10.1128/JB.00320-12;
RA Chouaia B., Crotti E., Brusetti L., Daffonchio D., Essoussi I., Nouioui I.,
RA Sbissi I., Ghodhbane-Gtari F., Gtari M., Vacherie B., Barbe V., Medigue C.,
RA Gury J., Pujic P., Normand P.;
RT "Genome Sequence of Blastococcus saxobsidens DD2, a Stone-Inhabiting
RT Bacterium.";
RL J. Bacteriol. 194:2752-2753(2012).
RN [2] {ECO:0000313|Proteomes:UP000007517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD2 {ECO:0000313|Proteomes:UP000007517};
RA Genoscope.;
RT "Complete genome sequence of Blastococcus saxobsidens strain DD2.";
RL Submitted (FEB-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 -!- 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}.
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DR EMBL; FO117623; CCG03248.1; -; Genomic_DNA.
DR AlphaFoldDB; H6RVH3; -.
DR STRING; 1146883.BLASA_2344; -.
DR KEGG; bsd:BLASA_2344; -.
DR eggNOG; COG1559; Bacteria.
DR HOGENOM; CLU_024739_0_0_11; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000007517; 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; 3.30.1490.480; 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:UP000007517};
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 238..258
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 1..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 459
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 580 AA; 60721 MW; D784AA64FBA3BCC5 CRC64;
MTAPGGLPRR GRHSFDGALG GGSSSFRTGP GASAGHGFPP GLGRGTAHED ATGPMVEPAW
WSFGSTDDPG SPLTARHGGG DEHGYGRQHP SAPLPPLPTG AWDRLRPRPE PGDDDATVAA
PRFAGKPDDE FPEDDAPTTG GPLWDEETGG LDVIGANVDE DRPRRRGFRR GPGAAVPPAP
VVDGAAAPEP GVADAPAGHD GDLLDTSGAG GHDPVADDEI PVEPYDSRSD RRRRRRPFAV
VLALLVLGAL VAGIVIGGQQ LLSLINPAAQ DYTGAGTGSI DVRVQEGDTL SDIARTLADA
DVIASTGPFV SAAEANPEAT GIQPGVYTLR LQMSGESALE MLLDPASRQV SRVTVPEGFT
VEQILARLAE ETGTPLEELQ AAADPAVLRL PAYAGGQLEG FLFPATYDFE PGTTPQQMLQ
RMVDTFTEVA GRLRLEERAA ALGLSPYEVV TVASMVQSET RLDEERADVA QVIYNRLEQG
IRLGIDATLA YGLDKSGNEL TVTDLETDSP YNTRTRAGLP PTPISSPGEA SLEAALAPTS
GDLLYYVLES QEGSHFFTSD YAEFQQARQR CADAGLGCGG
//
