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Database: UniProt
Entry: F0ENA3_ENTCA
LinkDB: F0ENA3_ENTCA
Original site: F0ENA3_ENTCA 
ID   F0ENA3_ENTCA            Unreviewed;       447 AA.
AC   F0ENA3;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   24-JAN-2024, entry version 40.
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=HMPREF9087_2895 {ECO:0000313|EMBL:EGC68305.1};
OS   Enterococcus casseliflavus ATCC 12755.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=888066 {ECO:0000313|EMBL:EGC68305.1, ECO:0000313|Proteomes:UP000004835};
RN   [1] {ECO:0000313|EMBL:EGC68305.1, ECO:0000313|Proteomes:UP000004835}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12755 {ECO:0000313|EMBL:EGC68305.1,
RC   ECO:0000313|Proteomes:UP000004835};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (JAN-2011) 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:EGC68305.1}.
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DR   EMBL; AEWT01000030; EGC68305.1; -; Genomic_DNA.
DR   AlphaFoldDB; F0ENA3; -.
DR   HOGENOM; CLU_025574_1_1_9; -.
DR   Proteomes; UP000004835; 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   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        94..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            329
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ   SEQUENCE   447 AA;  50036 MW;  D80D72757D0258B0 CRC64;
     MSKQHPEDKS FKDEVLGALK QPQSDQTQED HGLNERPIQQ PQEEVGSRTA SGKTKNKQAK
     QAATSRRAAA EEVPIAEGGE TQLRKQQRKK EDRIVNRIVL IVVLALLVIG GVLGFSMYRY
     VTSGLQPLNP EDTETVAVEI PSGSSNKAIG EILEEDNIIK SGMIFNYYTK FNNLTGFQAG
     NYHFSPSMTL DQISKMLQNG EGSVTSDAKV TIPEGFDVDQ IGDALAEATN ISKDDFLALM
     ESDEFFEKMK ETYPELLASA GDAQGVRYRL EGYLFPATYD YYTGNTLEEV VTQMVDKSNS
     VLSKYFDQIA QKEMTVQEVL TLASLVEKEG SKLEDRKNIA QVFFNRLAID MPLQSDISIL
     YALGEHKELV TYEDTQVDSP YNLYVHTGYG PGPFNNPSEA AIQAVLDPTP NNYYYFVADI
     QTQEVYFAET YEQHMQLVEQ YVNNTSN
//
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