ID S1P4Q7_9ENTE Unreviewed; 473 AA.
AC S1P4Q7;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
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=OMK_01213 {ECO:0000313|EMBL:EOT41045.1};
OS Enterococcus dispar ATCC 51266.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1139219 {ECO:0000313|EMBL:EOT41045.1, ECO:0000313|Proteomes:UP000014127};
RN [1] {ECO:0000313|EMBL:EOT41045.1, ECO:0000313|Proteomes:UP000014127}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51266 {ECO:0000313|EMBL:EOT41045.1,
RC ECO:0000313|Proteomes:UP000014127};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Enterococcus dispar ATCC_51266 (Illumina only
RT assembly).";
RL Submitted (MAR-2013) 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}.
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:EOT41045.1}.
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DR EMBL; AHYR01000005; EOT41045.1; -; Genomic_DNA.
DR RefSeq; WP_016172391.1; NZ_KE136354.1.
DR AlphaFoldDB; S1P4Q7; -.
DR STRING; 44009.RV01_GL002250; -.
DR PATRIC; fig|1139219.3.peg.1173; -.
DR eggNOG; COG1559; Bacteria.
DR HOGENOM; CLU_025574_1_1_9; -.
DR OrthoDB; 9814591at2; -.
DR Proteomes; UP000014127; 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 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 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:UP000014127};
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 122..146
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 1..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 36..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 358
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 473 AA; 53084 MW; CD0DE802E80EA675 CRC64;
MSKQHPEEES FKDKILNSLN NSDEGTSKEK RSSNRQGQQN KNSQSKNQRE RLNVSQESVG
SRRSSGAKDS FQNTKKESTE KKKAPVKKKP KNEKMSNATK PTLSVSADEM QRRKMRQKED
RIVSKIVTVV VLALLVIGGI LGFSVYRYVS SSLQPLDPDN KKTVAVEIPS GSSNKQIGEI
LQEDKVIKSG MVFNYYTKFN NLTGFQAGSY HFSPSMSLDD ISKNLQGGGA GTAGADAKLT
IPEGVDIDKI GDIIAKDTKI KKSDFLDLMK NEDFFKKMQE KYPDLLTSAA KAKGVRYRLE
GYLFPATYDY YKTSSLEDIV TQMIDKTNTV MSAYYDTIKQ KNMDVQEVIT LASLVEKEGV
TETDRKKIAQ VFFNRIAAGM PLQSDISILY ALGEHKEKVY NKDLQVDSPY NLYTNTGYGP
GPFDSPSEQS IKAVLDPTAN NYYYFVADIK TGKVYYAETY EEHLALVEKY VNN
//
