ID D5UE93_CELFN Unreviewed; 803 AA.
AC D5UE93;
DT 13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT 13-JUL-2010, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Glycosyl transferase family 51 {ECO:0000313|EMBL:ADG76569.1};
GN OrderedLocusNames=Cfla_3701 {ECO:0000313|EMBL:ADG76569.1};
OS Cellulomonas flavigena (strain ATCC 482 / DSM 20109 / BCRC 11376 / JCM
OS 18109 / NBRC 3775 / NCIMB 8073 / NRS 134).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=446466 {ECO:0000313|EMBL:ADG76569.1, ECO:0000313|Proteomes:UP000000849};
RN [1] {ECO:0000313|EMBL:ADG76569.1, ECO:0000313|Proteomes:UP000000849}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 482 / DSM 20109 / BCRC 11376 / JCM 18109 / NBRC 3775 /
RC NCIMB 8073 / NRS 134 {ECO:0000313|Proteomes:UP000000849};
RX PubMed=21304688; DOI=10.4056/sigs.1012662;
RA Abt B., Foster B., Lapidus A., Clum A., Sun H., Pukall R., Lucas S.,
RA Glavina Del Rio T., Nolan M., Tice H., Cheng J.F., Pitluck S., Liolios K.,
RA Ivanova N., Mavromatis K., Ovchinnikova G., Pati A., Goodwin L., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Rohde M.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Cellulomonas flavigena type strain (134).";
RL Stand. Genomic Sci. 3:15-25(2010).
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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001964; ADG76569.1; -; Genomic_DNA.
DR RefSeq; WP_013118896.1; NC_014151.1.
DR AlphaFoldDB; D5UE93; -.
DR STRING; 446466.Cfla_3701; -.
DR CAZy; GT51; Glycosyltransferase Family 51.
DR KEGG; cfl:Cfla_3701; -.
DR eggNOG; COG0744; Bacteria.
DR HOGENOM; CLU_006354_6_2_11; -.
DR OrthoDB; 9766909at2; -.
DR Proteomes; UP000000849; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004180; F:carboxypeptidase activity; 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:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd06577; PASTA_pknB; 1.
DR Gene3D; 3.30.10.20; -; 1.
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; IPR005543; PASTA_dom.
DR InterPro; IPR036950; PBP_transglycosylase.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR PANTHER; PTHR32282; BINDING PROTEIN TRANSPEPTIDASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR32282:SF34; PENICILLIN-BINDING PROTEIN 1A; 1.
DR Pfam; PF03793; PASTA; 1.
DR Pfam; PF00912; Transgly; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51178; PASTA; 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:UP000000849};
KW Transferase {ECO:0000313|EMBL:ADG76569.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 50..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 696..763
FT /note="PASTA"
FT /evidence="ECO:0000259|PROSITE:PS51178"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..701
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..803
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 803 AA; 85907 MW; 63627C55D82470F3 CRC64;
MAASNRRAAP SRARRATRRT APSARERQGF WNYPRREHTG LHRWLPSWRV VLGTFIGMIF
LVLGAGVAAF ALIKQDSPLA EVNYQTTTVY FAGPEPGTPG EVMGTFADQR RELVDYGTLP
EHIGQAVAAG EDKTFFTNSG ISLSGMARAF INNIQGKPTQ GGSTLTQQYV ERYYQDSTTD
YWGKAKEAII AIRIARTESK EMIMGRYLNT IYFGRDSYGI QAAAQSYFKV DAKDLTVAQA
ALLAAVIPSP NNWDPANDRP KAEQRWNIIL DRMVEMEWLT AEERAAQTFP PFEVYQESET
YRGPNGYLLK MVEKELVATK FWTEGELKTA GLKVLTTIDP ALQQMAVESA EGLRTGALSD
GAVPHERLRV SISTVDPATG GIVALYGGPD YLTDTRNTAT FDKVPAASTF KPFTLVAALQ
QGTSLATTYN GDSPQSFPQW ENGKPVPNYP NRDYGPIDLV RATADSVNTV YAQLNIQVGA
DNTKKVAETA GITTPLETNI SNVLGTDFVH PIDMAGAYAT FAAQGVRRAP HIVQQVNDSS
GAVAWQPDTT GQNVFPADVM ADATYAMTQV VEQGSGKAQV SRLDRPIAGK TGSETLNKGA
WFVGYVPQLS TAVSLSQLAE DGKGLDSIDG WGQFSSVNGS TFPALLWADY MGKVFADPRY
QEIQQFPPRA NVGKKPTVTA SATPTEVAPT AEETQAPAET QVPSGLAGRT EADASGALQG
AGLVARIANE RSATVPAGRV IRVEPGEGTT LAAGATVTLV VSSGAPQPTP SPTPPPAPSP
TPEPTQSAPP PDAGGGQQPP PNG
//
