ID   A0A2N0UPV8_9FIRM        Unreviewed;       451 AA.
AC   A0A2N0UPV8;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   20-JUN-2018, entry version 3.
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=RB5AMG_01336 {ECO:0000313|EMBL:PKD29033.1};
OS   Ruminococcus bromii.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Ruminococcaceae;
OC   Ruminococcus.
OX   NCBI_TaxID=40518 {ECO:0000313|EMBL:PKD29033.1, ECO:0000313|Proteomes:UP000233562};
RN   [1] {ECO:0000313|EMBL:PKD29033.1, ECO:0000313|Proteomes:UP000233562}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5AMG {ECO:0000313|EMBL:PKD29033.1,
RC   ECO:0000313|Proteomes:UP000233562};
RX   PubMed=29159997;
RA   Mukhopadhya I., Morais S., Laverde-Gomez J., Sheridan P.O.,
RA   Walker A.W., Kelly W., Klieve A.V., Ouwerkerk D., Duncan S.H.,
RA   Louis P., Koropatkin N., Cockburn D., Kibler R., Cooper P.J.,
RA   Sandoval C., Crost E., Juge N., Bayer E.A., Flint H.J.;
RT   "Sporulation capability and amylosome conservation among diverse human
RT   colonic and rumen isolates of the keystone starch-degrader
RT   Ruminococcus bromii.";
RL   Environ. Microbiol. 0:0-0(2017).
CC   -!- FUNCTION: Functions as a peptidoglycan terminase that cleaves
CC       nascent peptidoglycan strands endolytically to terminate their
CC       elongation. {ECO:0000256|HAMAP-Rule:MF_02065}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_02065}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC       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
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:PKD29033.1}.
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DR   EMBL; NNBY01000036; PKD29033.1; -; Genomic_DNA.
DR   Proteomes; UP000233562; Unassembled WGS sequence.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
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; YceG.
DR   PANTHER; PTHR30518; PTHR30518; 1.
DR   Pfam; PF02618; YceG; 1.
DR   TIGRFAMs; TIGR00247; TIGR00247; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_02065};
KW   Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02065};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000233562};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_02065, ECO:0000313|EMBL:PKD29033.1};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_02065};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_02065};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_02065}.
FT   TRANSMEM     92    111       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_02065}.
FT   COILED       57     88       {ECO:0000256|SAM:Coils}.
FT   SITE        330    330       Important for catalytic activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_02065}.
SQ   SEQUENCE   451 AA;  51899 MW;  A4C6C31E50848613 CRC64;
     MNPDNFNMNE QELNAQRRRR AENFKLNIDE SEYEDDNFIK SEDEPSNLNS YSGQDVKKQM
     ARESKQVLKQ KKKEEKKALK AKNKYNRRTF RFIWIISVLI VGAMAAVYMI TGMNDLLAVN
     RTDSSTVKIE IPENPTVDDV TKVLVDNKVI GEPSYFKLFV NVTKSADDFT QGTYEIRRNM
     DYEAIINFLS SSNNRTDTVS VTITEGESVL EIANTLEKNG ALGDRDEFLS LCNSEKFDSD
     FDFIKAETNA DKRYYKLEGY LYPDTYEFYR NENAESVIYK FLNNYETKIN EKQTVDGYSK
     KTTVLKMVEE SDTKYSLDQV MTIASIIQAE AADKEDMYYI SSILHNRLTA DSSLGVSSLG
     LDSTKFYPYR SLEDVPENDR STYKSRYDTY DRKGLPYGSI CNPGMDAIIA ALNPNSSDYY
     FFCHDSKGQA YYASTLEQQN ANLEYIESYD N
//