ID V6Q7I0_9ENTE Unreviewed; 388 AA.
AC V6Q7I0;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=T233_00007 {ECO:0000313|EMBL:EST90737.1};
OS Vagococcus lutrae LBD1.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=1408226 {ECO:0000313|EMBL:EST90737.1, ECO:0000313|Proteomes:UP000018126};
RN [1] {ECO:0000313|EMBL:EST90737.1, ECO:0000313|Proteomes:UP000018126}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LBD1 {ECO:0000313|EMBL:EST90737.1,
RC ECO:0000313|Proteomes:UP000018126};
RX PubMed=24371201;
RA Lebreton F., Valentino M.D., Duncan L.B., Zeng Q., Manson McGuire A.,
RA Earl A.M., Gilmore M.S.;
RT "High-Quality Draft Genome Sequence of Vagococcus lutrae Strain LBD1,
RT Isolated from the Largemouth Bass Micropterus salmoides.";
RL Genome Announc. 1:e01087-13(2013).
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:EST90737.1}.
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DR EMBL; AYSH01000001; EST90737.1; -; Genomic_DNA.
DR AlphaFoldDB; V6Q7I0; -.
DR STRING; 1408226.T233_00007; -.
DR PATRIC; fig|1408226.3.peg.7; -.
DR eggNOG; COG1559; Bacteria.
DR Proteomes; UP000018126; 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; 3.30.1490.480; 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:UP000018126};
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 37..60
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT SITE 271
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ SEQUENCE 388 AA; 44437 MW; A4FC0899992EBC57 CRC64;
MTLNISNVKL YRENESERSI MRREQAREKE NRLVRKIVTV VILSLVLIVT VLGIYIYKYW
QSGLKPLNPK DDHLVQVNIP IGTSNKGIGN ILEEQKIIKS GLVFTYYVKT ENITDFKGGY
YQMAPNMTLD EISEMLQQGG TEEPEALADA RITIPEGYSV DQIAKEVASK TGLKEDEILN
VITDEAFFKE LLASYPQLLQ SASEAQDVRF KLEGYLFPAT YNYYKDKGVK PLIQAMVEQM
NQVYIEREEM FNQSDLTVQQ VLTLASLVEK EGVENEDRRN IAGVFLNRIA ADMPLQSDIS
ILYAMDKHKV HLSNKDTEID SPYNLYINKG FGPGPFNNPS TDAIDAVLNP LENDYYYFLA
DITTHKVYFA ETYEKHLELK EQYIDNLQ
//
