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Database: UniProt
Entry: R5XCR8_9FIRM
LinkDB: R5XCR8_9FIRM
Original site: R5XCR8_9FIRM 
ID   R5XCR8_9FIRM            Unreviewed;       415 AA.
AC   R5XCR8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, 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=BN695_00929 {ECO:0000313|EMBL:CDA12640.1};
OS   Anaerotruncus sp. CAG:528.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Anaerotruncus.
OX   NCBI_TaxID=1262700 {ECO:0000313|EMBL:CDA12640.1, ECO:0000313|Proteomes:UP000018024};
RN   [1] {ECO:0000313|EMBL:CDA12640.1, ECO:0000313|Proteomes:UP000018024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:528 {ECO:0000313|Proteomes:UP000018024};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-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:CDA12640.1}.
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DR   EMBL; CBBE010000026; CDA12640.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5XCR8; -.
DR   STRING; 1262700.BN695_00929; -.
DR   Proteomes; UP000018024; 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   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:UP000018024};
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        59..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            288
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ   SEQUENCE   415 AA;  45998 MW;  706D6E987C6320E2 CRC64;
     MPDNFKKEEN GVNIGNADSP KKDIYFTNQD YSGVKTDKKP AAKAVSKAKG KKGGVASTYW
     FFIIVIAVSM VISVYAIFCL NDIFGITKSK DSVTVSYAQE IDNTSDAVDV LAENHLIKCK
     NFCKFYIKLA SKVVGSYDIE APFQAGVYYL NGKMGLEGML TSMMGTPETT ETVKVMIPEG
     YTVPEIIDKL VENEVCDKAA LLSVIDSTEF SYSLVSGLKA KESVPYRLEG YLFPDTYEFY
     VGQSASSVIE KFLEQTEKQI PEEYRKRAQE MGYSMNEIIT IASIVQAEAG SNDQMKTIAA
     VIENRLQDTT NYPSLGCQST TDYINNKVAP ALSSTSAHTA DYYLTYYSTA STSTVKGLPE
     GPICNPGKAA IEAVLYPEDN DDYFFFHDNN GKLYTAKTYS EFKSQIQKYA PYLSY
//
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