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Database: UniProt
Entry: C9A8D9_ENTCA
LinkDB: C9A8D9_ENTCA
Original site: C9A8D9_ENTCA 
ID   C9A8D9_ENTCA            Unreviewed;       773 AA.
AC   C9A8D9;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 2.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=peptidoglycan glycosyltransferase {ECO:0000256|ARBA:ARBA00012555};
DE            EC=2.4.1.129 {ECO:0000256|ARBA:ARBA00012555};
GN   ORFNames=ECBG_01019 {ECO:0000313|EMBL:EEV38750.2};
OS   Enterococcus casseliflavus EC20.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=565655 {ECO:0000313|EMBL:EEV38750.2, ECO:0000313|Proteomes:UP000012675};
RN   [1] {ECO:0000313|EMBL:EEV38750.2, ECO:0000313|Proteomes:UP000012675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC20 {ECO:0000313|EMBL:EEV38750.2,
RC   ECO:0000313|Proteomes:UP000012675};
RG   The Broad Institute Genome Sequencing Platform;
RA   Feldgarden M., Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L.,
RA   Berlin A., Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M.,
RA   Goldberg J., Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C.,
RA   Jen D., Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Walk T.,
RA   White J., Yandava C., Gilmore M., Manson J., Palmer K., Carniol K.,
RA   Lander E., Nusbaum C., Galagan J., Birren B.;
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EEV38750.2, ECO:0000313|Proteomes:UP000012675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EC20 {ECO:0000313|EMBL:EEV38750.2,
RC   ECO:0000313|Proteomes:UP000012675};
RG   The Broad Institute Genomics Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Russ C., Feldgarden M., Gilmore M., Manson J., Palmer K., Carniol K.,
RA   Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA   Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Enterococcus casseliflavus EC20 (899205).";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-
CC         Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-
CC         (1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-
CC         cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-
CC         D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl
CC         diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+);
CC         Xref=Rhea:RHEA:23708, Rhea:RHEA-COMP:9602, Rhea:RHEA-COMP:9603,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58405, ChEBI:CHEBI:60033,
CC         ChEBI:CHEBI:78435; EC=2.4.1.129;
CC         Evidence={ECO:0000256|ARBA:ARBA00023988};
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DR   EMBL; CP004856; EEV38750.2; -; Genomic_DNA.
DR   AlphaFoldDB; C9A8D9; -.
DR   KEGG; ecas:ECBG_01019; -.
DR   eggNOG; COG0744; Bacteria.
DR   HOGENOM; CLU_006354_2_5_9; -.
DR   Proteomes; UP000012675; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.3810.10; Biosynthetic peptidoglycan transglycosylase-like; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR001264; Glyco_trans_51.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR036950; PBP_transglycosylase.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   NCBIfam; TIGR02074; PBP_1a_fam; 1.
DR   PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR32282:SF29; PENICILLIN-BINDING PROTEIN 1A; 1.
DR   Pfam; PF00912; Transgly; 1.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012675};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        37..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          88..264
FT                   /note="Glycosyl transferase family 51"
FT                   /evidence="ECO:0000259|Pfam:PF00912"
FT   DOMAIN          358..649
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          682..773
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        14..28
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        682..756
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        757..773
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   773 AA;  84372 MW;  6E3B08A5CC5DB133 CRC64;
     MANGSQSRTS RHDSKKGTAK KAPKPPKAKG KRSIGSILLK VFMGLFFLGC IGILSGMGLF
     WWYAKDAPAL DETRLDSTVS SRFYASNGEL ITEFGSETRE KITASEIPQL LEDAIVSVED
     RRFYQHIGVD PIRIVGSALS NATTGGMQGG STLTQQLIKL SFFSTSAEDQ TLRRKAQEAW
     MAVRLEQMKS KQEILTYYIN KVYMSNGVYG MQTAAMKFYG KPLAELDLAQ TALIAGLPNA
     PSAFDPFAHP DNAKSRRDVV LGAMLENEKI TQAEYDAAVA EDIQEGLQDN PRENQEWKYF
     DNYFNEVIAE VKEKTGKDVY TDGLDIYTNV DIDAQKRLYD IVNSDDYVDY PDDKMQVAAT
     LVDVNTGKVT AQIGARNVDD VLANNLAVNV ARDFGSTVKP ITDYGPAFQF LQDSTGRMIL
     DEPYTYKGTN IPVYNWDRQY MGNITLRTAL AESRNVPAVK LFDEVGADNI ADFLSGLGIE
     YDTITQSNAI SSNTDKLDGT KYGISSLKMA AAYAAFSNGG TYYEPQYVNK IVMQDGTEDE
     ESFKVSGQEA MDDTTAYMVT DILKDVISVG TGTNAQIDGL YQAGKTGTSN YTDDQLAQLD
     TSNGAYPDIT FAGYTPSYSL AVWTGYNDKM TPITDSSTHV ASDVYRELMR YVSASVENTD
     WTMPDGLTRI GRELYLEGTY TQPSYSAPSS SSSSSYVEPT TPSTESSEST PSSTTESSSE
     VTPPVTTPDE DDSSSVVTPP ASSQDPGSTT PSSSEENPSS PPDPPEPNDG SVE
//
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