ID B5AGT2_CLOPF Unreviewed; 1779 AA. AC B5AGT2; DT 23-SEP-2008, integrated into UniProtKB/TrEMBL. DT 23-SEP-2008, sequence version 1. DT 27-MAR-2024, entry version 36. DE SubName: Full=TpeL {ECO:0000313|EMBL:ACF49258.1}; GN Name=tpeL {ECO:0000313|EMBL:ACF49258.1}; OS Clostridium perfringens A. OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=37763 {ECO:0000313|EMBL:ACF49258.1}; RN [1] {ECO:0000313|EMBL:ACF49258.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CP4 {ECO:0000313|EMBL:ACF49258.1}; RA Chalmers G., Bruce H.L., Hunter B., Parreira V.R., Kulkarni R.R., RA Jiang Y.-F., Prescott J.F., Boerlin P.; RT "Multilocus Sequence Typing Analysis of Clostridium perfringens Isolates RT from Necrotic Enteritis Outbreaks in Broiler Chickens."; RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACF49258.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=CP4 {ECO:0000313|EMBL:ACF49258.1}; RX PubMed=19848081; DOI=10.1637/8656-021109-Reg.1; RA Jiang Y., Kulkarni R.R., Parreira V.R., Prescott J.F.; RT "Immunization of broiler chickens against Clostridium perfringens-induced RT necrotic enteritis using purified recombinant immunogenic proteins."; RL Avian Dis. 53:409-415(2009). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946}; CC -!- SUBCELLULAR LOCATION: Host cytoplasm, host cytosol CC {ECO:0000256|ARBA:ARBA00023586}. Membrane CC {ECO:0000256|ARBA:ARBA00004370}. Secreted CC {ECO:0000256|ARBA:ARBA00004613}. 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; EU848493; ACF49258.1; -; Genomic_DNA. DR SMR; B5AGT2; -. DR CAZy; GT44; Glycosyltransferase Family 44. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0044164; C:host cell cytosol; IEA:UniProtKB-SubCell. DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016757; F:glycosyltransferase activity; IEA:InterPro. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW. DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW. DR CDD; cd20502; C80_toxinA_B-like; 1. DR CDD; cd16840; toxin_MLD; 1. DR Gene3D; 1.10.10.1780; -; 1. DR Gene3D; 1.10.274.80; -; 1. DR Gene3D; 1.10.3730.30; -; 1. DR Gene3D; 1.20.58.1190; -; 1. DR Gene3D; 3.40.50.11050; -; 1. DR InterPro; IPR020974; CPD_dom. DR InterPro; IPR038383; CPD_dom_sf. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR024770; TcdA/TcdB_cat. DR InterPro; IPR024772; TcdA/TcdB_N. DR InterPro; IPR024769; TcdA/TcdB_pore_forming. DR Pfam; PF11713; Peptidase_C80; 1. DR Pfam; PF12919; TcdA_TcdB; 1. DR Pfam; PF12920; TcdA_TcdB_pore; 1. DR Pfam; PF12918; TcdB_N; 1. DR SUPFAM; SSF53448; Nucleotide-diphospho-sugar transferases; 1. DR PROSITE; PS51771; CGT_MARTX_CPD; 1. PE 4: Predicted; KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511}; KW Host cytoplasm {ECO:0000256|ARBA:ARBA00023200}; KW Host membrane {ECO:0000256|ARBA:ARBA00022511}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842}; KW Membrane {ECO:0000256|ARBA:ARBA00023136}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Protease {ECO:0000256|ARBA:ARBA00022670}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Toxin {ECO:0000256|ARBA:ARBA00022656}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}; KW Virulence {ECO:0000256|ARBA:ARBA00023026}. FT DOMAIN 568..772 FT /note="Peptidase C80" FT /evidence="ECO:0000259|PROSITE:PS51771" SQ SEQUENCE 1779 AA; 206288 MW; 7D78D5890807133A CRC64; MGLMSKEQLI ILAKNSSPKE GEYKKILELL DEYNLLNNSV EKNSIDLYLK LNELSKSIDI YLKKYKNSKR NNALYQLKSD LTKEVIEIKD INLKPLEKNI HFVWVGGMIN NISIDYINQW KDINSDYETI IWYDSEALLV NILKKAIIDS SNKEVLTKYE SVLNDNSFDS NKFYRERMEV IFRKQKEFNN YYNTNDNYTK SLNDVIKVYL IEKYLKTDEE LEKYINESKE VFKANGAKDI REYDILDDVE LKSIYEQELL MRFNLAAASD IIRVIVLNKL GGIYLDVDVL PGIKKHIFKD INKPTNISEN KWQMIQLETI MKYKQYIKGY TENSFKNLPS DLQEILQEKV VEKNLKSDIF QRLGDIFISE LDTKIAFMFG KIANQVLISK KNSYSLNLII NQIKNRYNII NKCLSSAIEK GSNFNNTVDI FIQQLNEFYV NEGFFVSKVM GYLGDGYMPD MRATLNISGP GIYTAAYYDL LYFNERSLNP QILQEDLKYF EVPQALISQQ TEQEINSSWT FNQVKSQIEY KKLVEKYTNK SLSENDKLNF NENKIIDKVE LLNRINSNNL INFDDKEYLR YIIQLQGDKV SYEAAINLFI KNPSNSILVQ EINNISYYFN SEYKSIDSIQ FDNIPEILKG KNKIKLTFIG HGEEEFNTER FASLTVKEFS KKIYKVLDII KSNTNVKEIQ IDLLGCNMFS YNINVEETYP GKLLKVVLDY VDKIYNADIK PEIKISANQY EVRINKDGKK ELLSHSGEWL SKEEAIIKDI ASKEIIYFDT RENTIKAESK NIMELITFRN SLDKKLNDLE SLINNNFIVN EVYEQLTSNN LYRTSFRNSF LDTINFIEDI SQELYEIKIK NNINDDYIIS LDEIKQDNNI SKIKFININS GEFRVVRENS RLINKFKEDF KFTINNLKRL INFTDNNKLI TSFELKNIEA SSGVSTLNTS FLIPSMIDYK AHNFDFNKLS TSVKVQIYCQ ITNISLSEIQ DASNLVKIIA EANEIEINLI PTLANAIPLI TTIVDGINLI ANIDELINTK DELIKKELAA RIGVISSNMT AAISSYILYF TEFGEVFNPL LVPIAGISSG IPTLINNILI LEEKSKEITE YFSHISKVES DGLFKVSDNN SILIPLDDIA ISKIDFNERK VILDKLDIWA MEGGSGLSGK ETFFSAPYVN ENLPKLSIDN LLKIDINKID FSIKGMMLPN GISKTLGYEF NTVDNIYELE NDGVNLLNRI RDNYPGQFYW RYYSTLFNYG MVNLKINYHD TDVKINLDNA DRMFIVPTLT IDQAREKLSY NFNGAGANYY IYFSSQPIKI FINGTKEDNW ILNIDDIVKE VTIVNNSIVR GNFIENIFEK LTIEDNKIII GNQKIYLKNN KTNIHFSVSI LDGVNLMVEV DFNNKMYHLS LQGNEKTICN NMNIIQNNIN KLFGSSSIKS IPYFYKNNGL ENFIGVFSIK NNEFIYMLKD GDKNEIYKYK DNNLVCSFNL FNISYVDIIS NGDKNYLKGI WNTSINNSEY KIEFLVELID QNTIEIIKLN LSDELIKSFL TILDNLENLD VKISTIYDFL KNILFRDVFL ENESLNFIVS KGFILTGNSS KNKYEFICNG ENIQLYIAEL YTNCTKFRNW LDNGKILVSS TDESSNNLIE YNENILSGLY SFINDIIINL DNGVEEINIL LNDNSESFYK NIIINSFKNL RNEIKLKINV DYNDFKWYIK GNDIILVRKK INGFNSTILL KDTVDNNSYF NYVTLIFNDK SIKLNNIIFE MEPIIGYRD //