ID I2JC87_9STRE Unreviewed; 586 AA.
AC I2JC87;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=HMPREF1116_0922 {ECO:0000313|EMBL:EIF40589.1};
OS Streptococcus sp. SK140.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1095726 {ECO:0000313|EMBL:EIF40589.1, ECO:0000313|Proteomes:UP000003237};
RN [1] {ECO:0000313|EMBL:EIF40589.1, ECO:0000313|Proteomes:UP000003237}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK140 {ECO:0000313|EMBL:EIF40589.1,
RC ECO:0000313|Proteomes:UP000003237};
RA Durkin A.S., McCorrison J., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (APR-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}.
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:EIF40589.1}.
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DR EMBL; AJML01000010; EIF40589.1; -; Genomic_DNA.
DR RefSeq; WP_001293910.1; NZ_AJML01000010.1.
DR AlphaFoldDB; I2JC87; -.
DR PATRIC; fig|1095726.3.peg.245; -.
DR eggNOG; COG1559; Bacteria.
DR Proteomes; UP000003237; 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 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 218..240
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT REGION 29..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 80..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 148..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 457
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 586 AA; 64544 MW; CD390FFD771F9CDE CRC64;
MSENSREEEK LSFKEQILRD LERLKREDGI ANTKSSNDDL FSNLNNSSEA EKSVEEPSVE
DLMANSVSLV DELLANAPAV PPRPVLQDDS VETSVASEPV VASEPTVASE PAVAPDPLPS
TEAVEPVKPL EPAQPAEEEK EFNAISTRIP VSYRTNQAKP SPARKNIKPQ PKPTVLAKET
PSQEPVAPVE TRTELPRRSR KESVKPIKKK KKSRLKGFFV TVFVLLILLG VGGFFGYRYV
ESALQPVDAN SKQYVTVQIP EGANLQQIGD TLENSGLVKH GFIFSLYAKY KDYNDLKSGY
YNLQKSMSTD DIIKELQKGG TPQPQEVALA NLTIPEGYTL DQIAQTVGQL QGDFKEPLTA
DAFLAKVQDE TFISQLVAKY PTLLESLPTK ESGVRYRLEG YLFPATYAIK ESTTIESLID
EMVAAMDKNL SAHYTAIKEK NLTVNELLTI ASLVEKEGLK TDDRKLIAGV FYNRLNLGMP
LQSNIAILYA EGKLGQNISL ADDAAIDTTI NSPYNVYTNL GLMPGPVDSP SLDAIEASIN
QTKSDYLYFV ANVQDGKVYF ATTREEHDRN VAEHVNSKLT QSSSSN
//
