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Database: UniProt
Entry: J8ZZE7_ENTFC
LinkDB: J8ZZE7_ENTFC
Original site: J8ZZE7_ENTFC 
ID   J8ZZE7_ENTFC            Unreviewed;       391 AA.
AC   J8ZZE7;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   13-SEP-2023, entry version 29.
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=HMPREF1345_00835 {ECO:0000313|EMBL:EJV55460.1};
OS   Enterococcus faecium TX1337RF.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1134802 {ECO:0000313|EMBL:EJV55460.1, ECO:0000313|Proteomes:UP000003117};
RN   [1] {ECO:0000313|EMBL:EJV55460.1, ECO:0000313|Proteomes:UP000003117}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX1337RF {ECO:0000313|EMBL:EJV55460.1,
RC   ECO:0000313|Proteomes:UP000003117};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (APR-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:EJV55460.1}.
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DR   EMBL; AMAA01000033; EJV55460.1; -; Genomic_DNA.
DR   RefSeq; WP_002347960.1; NZ_JH804714.1.
DR   AlphaFoldDB; J8ZZE7; -.
DR   PATRIC; fig|1134802.3.peg.779; -.
DR   HOGENOM; CLU_025574_1_1_9; -.
DR   Proteomes; UP000003117; 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; 3.30.160.60; 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 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        41..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
FT   SITE            275
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02065"
SQ   SEQUENCE   391 AA;  44245 MW;  B4768F6758D3A9BD CRC64;
     MSGNKQHPSK DKKEASKAAT ADIIDKRRNL RKKEDKIVRK IILVIALTLL IIGGFLGFTV
     YRYVDSGLKP LDKSDDQLVQ VEIPSGSSNK QIGEILEKDN IIKSGIVFNY YTKFKNLTGF
     QAGYYQLAPN MTLDEIGKQL QEGGTSEPTK VADGKIAIPE GYDIDQIAER VAKVTVKDKK
     EFLDLVNDET FFNELHQKFP ELLESASKAE NTKYRLEGYL FPATYDYYTS TSLKDLVIEM
     VNKTNTVMQN YYSAIKQKNL TVQEVLTLAS LVEKEGVKEN DRKNIAQVFF NRIKANMPLQ
     SDISVLYALG EHKELVTYED TAVDSPYNLY TNTGYGPGPF DNPSEEAIKA VLEPAENDYY
     YFVADTSTGN VYFAKTYEEH MELVEKYVNN S
//
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