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Database: UniProt
Entry: A0A0P7XLR8_9RHOB
LinkDB: A0A0P7XLR8_9RHOB
Original site: A0A0P7XLR8_9RHOB 
ID   A0A0P7XLR8_9RHOB        Unreviewed;       387 AA.
AC   A0A0P7XLR8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=HLUCCA12_00120 {ECO:0000313|EMBL:KPQ08243.1};
OS   Rhodobacteraceae bacterium HLUCCA12.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1666916 {ECO:0000313|EMBL:KPQ08243.1, ECO:0000313|Proteomes:UP000050476};
RN   [1] {ECO:0000313|EMBL:KPQ08243.1, ECO:0000313|Proteomes:UP000050476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLUCCA12 {ECO:0000313|EMBL:KPQ08243.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (SEP-2015) 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   -!- 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:KPQ08243.1}.
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DR   EMBL; LJSV01000001; KPQ08243.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7XLR8; -.
DR   STRING; 1666916.HLUCCA12_00120; -.
DR   PATRIC; fig|1666916.3.peg.1787; -.
DR   Proteomes; UP000050476; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
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 inner membrane {ECO:0000256|HAMAP-Rule:MF_02065};
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   SITE            259
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ   SEQUENCE   387 AA;  42965 MW;  F483C22BA468D4D4 CRC64;
     MFRHVAANGM TLLIVGLLLL AAIMTMGQRV FQSEGPLEQA ICLRVEPGAT LRGVTRTLED
     EGAIRNAMIF RIGAQYTERD NQLRFGSYLV GPGASMDEIL DIITSGGAST CGTEVVLRIG
     VTEAEYRVRE LDPQTDRFEE VLTHPLDDED FPEAYDEVAE RADTRFRITI AEGATSWQVW
     NALTQAEFLS GDLPDVPDEG TLATESYELS RGAERSALVE EMQERQAAIL ADAWENRAPD
     LPLDSPDEAL ILASIVEKET GQPEERRQVA SVFINRLRLP MRLQTDPTVI YGITRGERSL
     GRGLRRSELD AETPYNTYRI EGLPPTPIAN PGRASIEAAL NPDETEYLYF VADGTGGHAF
     ATNLADHNRN VARWRAIEAE LEQERDQ
//
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