ID B1L2K5_CLOBM Unreviewed; 1206 AA.
AC B1L2K5;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE RecName: Full=Transglutaminase-like domain-containing protein {ECO:0000259|SMART:SM00460};
GN OrderedLocusNames=CLK_A0116 {ECO:0000313|EMBL:ACA57365.1};
OS Clostridium botulinum (strain Loch Maree / Type A3).
OG Plasmid pCLK {ECO:0000313|EMBL:ACA57365.1,
OG ECO:0000313|Proteomes:UP000000722}.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498214 {ECO:0000313|EMBL:ACA57365.1, ECO:0000313|Proteomes:UP000000722};
RN [1] {ECO:0000313|EMBL:ACA57365.1, ECO:0000313|Proteomes:UP000000722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Loch Maree / Type A3 {ECO:0000313|Proteomes:UP000000722};
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
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; CP000963; ACA57365.1; -; Genomic_DNA.
DR RefSeq; WP_012300901.1; NC_010418.1.
DR AlphaFoldDB; B1L2K5; -.
DR KEGG; cbl:CLK_A0116; -.
DR HOGENOM; CLU_275932_0_0_9; -.
DR Proteomes; UP000000722; Plasmid pCLK.
DR Gene3D; 3.10.620.30; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR002931; Transglutaminase-like.
DR PANTHER; PTHR33490; BLR5614 PROTEIN-RELATED; 1.
DR PANTHER; PTHR33490:SF3; SLL1049 PROTEIN; 1.
DR Pfam; PF01841; Transglut_core; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Plasmid {ECO:0000313|EMBL:ACA57365.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..1206
FT /note="Transglutaminase-like domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039483093"
FT DOMAIN 265..323
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
FT COILED 399..438
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 547..716
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 767..921
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1206 AA; 138606 MW; 18D6F251B70ECAAE CRC64;
MLSKKTKKLI TSAILSLTIS LSFLGTSITE VKAFDRTKAV YELKNARTYE YTWSYDISIN
RDVDYARGEI YLGSISSTAH QLDTTPFRVT MNGEPLKIFN STKNSLGEKE KELLDKEKDN
SYNKNKTFGI WQQELDGNFR LYVYVINATS GFNKTLKITK EFISGDLDYG LYNKDTKEFS
DKLKEVLNSS YDKSDLLKIY KYDIDPRDGT SKIPYHEKEI IDETKRVTKD CTNDMEKVQA
IYKFVVKHME YVEDPAYRNK GALSALKSGK GVCEDYASLF IAMCREVNIP ARYVHGLTGA
TGNHGWAEFY LPYYGWIIAE PTVSSLRTAN EDTLQKAMMT FIGTYDTNND FIPSHSVAGY
NNNEDRYHAI FDRIKVTNQN RIITIKGEPI KSVVYNQPFS NYQERIDSVN KLLEIAKNTK
KEEDIKEARE LAQTLIDSEE RENTLKQLSY IGKSDELKSQ IGELVVALEN SDTIDTNKFE
ELKEILNNAP EEIVSEFKTA YDKVQKRYEI ENLIKETEGN LTEENLDKLS NLLDNTNIED
KYKLSYISKY DKLLNDYTKK VEEQEQAKYQ AKLQAATKAV EKAETSKNQT DVDNARGLAN
SLKATDKSNL NARLDEIQKT IDDKKTEEEK QAEYQAKLQV ATKAVEKAEA SKNQADVDNA
KILVNSLKDT DKSNLNARLD EVQKAIDAKK TEEEKQAEYE AKVQTAIKAV EKAEKTTIYE
DYISATKLVS KLQISEIQTQ LWDRLREVKV DIGRKEEATE LVKLAEEDNT ETNYNRALES
INRLRDNELK QDLLNRLNNV KSNIDNNNAK KEEVNKLVAQ AEKDNKEETY NKALAAVQSL
EDDQLKKELL TRLNNVKSII DNNSKKEDVT KLVEQAEQDN KEETYNKALT AVKALEDSQA
KKDLLNRLDK VKVNIDKIKT NEAIRLVEYA EKYPSISTYN NAKDTVNSIN DSNTKTELLN
RLKNVEIKIE KLDEKTKTHQ FTDYVDNLVR EAEKLCTEDA YKKALEQAQK IEDVQSRKVY
INRLNEVKNN IDISKETETS PIKTELDNLE HAINSINTVN KNDILAIKEK INDLKNTKER
QDLIDKLNNI ENKYNKLINN PNYNKLIKYN TWNNIVYKES KDKTFAVKFN KNLNSNNISE
NLYLLDVDNN FEKIHTTINI KGETAYITAD KLSPGKKYIL VVSDQIKDSR NKDLKQGLKT
FIQIIE
//
