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P16154

- TOXA_PEPDI

UniProt

P16154 - TOXA_PEPDI

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Protein

Toxin A

Gene

toxA

Organism
Peptoclostridium difficile (Clostridium difficile)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

Functioni

Only after the enteral delivery of the enterotoxin A may the characteristic disease called pseudomembranous colitis be induced.

GO - Molecular functioni

  1. transferase activity, transferring glycosyl groups Source: InterPro

GO - Biological processi

  1. pathogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Enterotoxin, Toxin

Protein family/group databases

CAZyiGT44. Glycosyltransferase Family 44.
MEROPSiC80.002.
TCDBi1.C.57.1.2. the clostridial cytotoxin (cct) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Toxin A
Gene namesi
Name:toxA
Synonyms:tcdA
OrganismiPeptoclostridium difficile (Clostridium difficile)
Taxonomic identifieri1496 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptostreptococcaceaePeptoclostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 27102710Toxin APRO_0000072634Add
BLAST

Structurei

Secondary structure

1
2710
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 127Combined sources
Helixi21 – 3414Combined sources
Helixi41 – 6121Combined sources
Helixi68 – 8821Combined sources
Beta strandi95 – 1006Combined sources
Helixi108 – 12013Combined sources
Turni121 – 1233Combined sources
Beta strandi124 – 1307Combined sources
Helixi137 – 16024Combined sources
Helixi167 – 19226Combined sources
Helixi201 – 21212Combined sources
Helixi217 – 23216Combined sources
Turni233 – 2353Combined sources
Beta strandi236 – 2383Combined sources
Turni239 – 2435Combined sources
Helixi248 – 25811Combined sources
Turni259 – 2613Combined sources
Helixi264 – 27916Combined sources
Beta strandi281 – 2844Combined sources
Turni294 – 2996Combined sources
Helixi308 – 32316Combined sources
Helixi334 – 3363Combined sources
Helixi339 – 35012Combined sources
Helixi355 – 3573Combined sources
Beta strandi366 – 3683Combined sources
Beta strandi373 – 3775Combined sources
Beta strandi380 – 3889Combined sources
Helixi393 – 41725Combined sources
Turni418 – 4203Combined sources
Helixi423 – 43513Combined sources
Turni440 – 4423Combined sources
Helixi443 – 4497Combined sources
Helixi452 – 4543Combined sources
Turni455 – 4573Combined sources
Helixi464 – 4674Combined sources
Helixi470 – 48213Combined sources
Helixi494 – 4974Combined sources
Helixi498 – 5003Combined sources
Helixi504 – 5063Combined sources
Helixi512 – 5176Combined sources
Helixi523 – 53614Combined sources
Helixi558 – 5636Combined sources
Helixi565 – 5695Combined sources
Beta strandi578 – 5858Combined sources
Helixi590 – 60213Combined sources
Helixi604 – 6063Combined sources
Beta strandi607 – 6115Combined sources
Helixi612 – 6176Combined sources
Beta strandi619 – 6235Combined sources
Beta strandi630 – 6345Combined sources
Helixi640 – 6423Combined sources
Beta strandi646 – 6538Combined sources
Helixi670 – 68415Combined sources
Turni685 – 6873Combined sources
Beta strandi691 – 70111Combined sources
Helixi709 – 7113Combined sources
Helixi713 – 72816Combined sources
Helixi734 – 7363Combined sources
Beta strandi737 – 7415Combined sources
Beta strandi746 – 7483Combined sources
Beta strandi754 – 7574Combined sources
Helixi766 – 7716Combined sources
Beta strandi778 – 7836Combined sources
Turni784 – 7874Combined sources
Beta strandi788 – 7958Combined sources
Beta strandi2395 – 23973Combined sources
Beta strandi2399 – 24013Combined sources
Beta strandi2410 – 24123Combined sources
Beta strandi2424 – 24296Combined sources
Beta strandi2442 – 24454Combined sources
Beta strandi2448 – 24514Combined sources
Beta strandi2454 – 24574Combined sources
Beta strandi2462 – 24654Combined sources
Beta strandi2468 – 24725Combined sources
Beta strandi2474 – 24785Combined sources
Beta strandi2482 – 24865Combined sources
Beta strandi2489 – 24935Combined sources
Turni2495 – 24973Combined sources
Beta strandi2503 – 25075Combined sources
Beta strandi2510 – 25145Combined sources
Beta strandi2523 – 25275Combined sources
Beta strandi2530 – 25345Combined sources
Beta strandi2553 – 25586Combined sources
Beta strandi2561 – 25655Combined sources
Beta strandi2574 – 25785Combined sources
Beta strandi2581 – 25855Combined sources
Turni2587 – 25893Combined sources
Beta strandi2590 – 25934Combined sources
Beta strandi2595 – 25995Combined sources
Beta strandi2602 – 26076Combined sources
Beta strandi2614 – 26185Combined sources
Beta strandi2621 – 26266Combined sources
Beta strandi2644 – 26496Combined sources
Beta strandi2652 – 26565Combined sources
Beta strandi2660 – 26623Combined sources
Beta strandi2665 – 26695Combined sources
Beta strandi2672 – 26765Combined sources
Turni2678 – 26803Combined sources
Beta strandi2686 – 26916Combined sources
Beta strandi2694 – 26985Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2F6EX-ray1.85A2583-2709[»]
2G7CX-ray2.00A/B2456-2710[»]
2QJ6X-ray2.50A/B2387-2706[»]
3HO6X-ray1.60A/B543-809[»]
4DMVX-ray1.50A1-541[»]
4DMWX-ray2.50A1-541[»]
ProteinModelPortaliP16154.
SMRiP16154. Positions 1-542, 1862-1980, 2254-2706.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16154.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini583 – 768186Peptidase C80Add
BLAST
Repeati1810 – 182920Cell wall-binding 1Add
BLAST
Repeati1851 – 187020Cell wall-binding 2Add
BLAST
Repeati1872 – 189120Cell wall-binding 3Add
BLAST
Repeati1923 – 194220Cell wall-binding 4Add
BLAST
Repeati1943 – 196220Cell wall-binding 5Add
BLAST
Repeati1964 – 198320Cell wall-binding 6Add
BLAST
Repeati1985 – 200420Cell wall-binding 7Add
BLAST
Repeati2006 – 202520Cell wall-binding 8Add
BLAST
Repeati2057 – 207620Cell wall-binding 9Add
BLAST
Repeati2077 – 209620Cell wall-binding 10Add
BLAST
Repeati2098 – 211720Cell wall-binding 11Add
BLAST
Repeati2119 – 213820Cell wall-binding 12Add
BLAST
Repeati2140 – 215920Cell wall-binding 13Add
BLAST
Repeati2191 – 221020Cell wall-binding 14Add
BLAST
Repeati2211 – 223020Cell wall-binding 15Add
BLAST
Repeati2232 – 225120Cell wall-binding 16Add
BLAST
Repeati2252 – 227120Cell wall-binding 17Add
BLAST
Repeati2305 – 232420Cell wall-binding 18Add
BLAST
Repeati2325 – 234420Cell wall-binding 19Add
BLAST
Repeati2346 – 236520Cell wall-binding 20Add
BLAST
Repeati2367 – 238620Cell wall-binding 21Add
BLAST
Repeati2388 – 240720Cell wall-binding 22Add
BLAST
Repeati2439 – 245820Cell wall-binding 23Add
BLAST
Repeati2459 – 247820Cell wall-binding 24Add
BLAST
Repeati2480 – 249920Cell wall-binding 25Add
BLAST
Repeati2501 – 252020Cell wall-binding 26Add
BLAST
Repeati2552 – 257120Cell wall-binding 27Add
BLAST
Repeati2572 – 259120Cell wall-binding 28Add
BLAST
Repeati2593 – 261220Cell wall-binding 29Add
BLAST
Repeati2643 – 266220Cell wall-binding 30Add
BLAST
Repeati2663 – 268220Cell wall-binding 31Add
BLAST
Repeati2685 – 270420Cell wall-binding 32Add
BLAST

Domaini

The C-terminal part of toxin A consists of a 833 AA repetitive structure. This part of toxin A is composed of five different oligopeptides.

Sequence similaritiesi

Belongs to the peptidase C80 family.Curated
Contains 32 cell wall-binding repeats.PROSITE-ProRule annotation
Contains 1 peptidase C80 domain.Curated

Keywords - Domaini

Repeat

Family and domain databases

InterProiIPR018337. Cell_wall/Cho-bd_repeat.
IPR029044. Nucleotide-diphossugar_trans.
IPR020974. Pept_C80_RTX.
IPR024770. TcdA/TcdB_cat.
IPR024772. TcdA/TcdB_N.
IPR024769. TcdA/TcdB_pore_forming.
[Graphical view]
PfamiPF01473. CW_binding_1. 12 hits.
PF11713. Peptidase_C80. 1 hit.
PF12919. TcdA_TcdB. 1 hit.
PF12920. TcdA_TcdB_pore. 1 hit.
PF12918. TcdB_N. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
PROSITEiPS51170. CW. 32 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P16154-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSLISKEELI KLAYSIRPRE NEYKTILTNL DEYNKLTTNN NENKYLQLKK
60 70 80 90 100
LNESIDVFMN KYKTSSRNRA LSNLKKDILK EVILIKNSNT SPVEKNLHFV
110 120 130 140 150
WIGGEVSDIA LEYIKQWADI NAEYNIKLWY DSEAFLVNTL KKAIVESSTT
160 170 180 190 200
EALQLLEEEI QNPQFDNMKF YKKRMEFIYD RQKRFINYYK SQINKPTVPT
210 220 230 240 250
IDDIIKSHLV SEYNRDETVL ESYRTNSLRK INSNHGIDIR ANSLFTEQEL
260 270 280 290 300
LNIYSQELLN RGNLAAASDI VRLLALKNFG GVYLDVDMLP GIHSDLFKTI
310 320 330 340 350
SRPSSIGLDR WEMIKLEAIM KYKKYINNYT SENFDKLDQQ LKDNFKLIIE
360 370 380 390 400
SKSEKSEIFS KLENLNVSDL EIKIAFALGS VINQALISKQ GSYLTNLVIE
410 420 430 440 450
QVKNRYQFLN QHLNPAIESD NNFTDTTKIF HDSLFNSATA ENSMFLTKIA
460 470 480 490 500
PYLQVGFMPE ARSTISLSGP GAYASAYYDF INLQENTIEK TLKASDLIEF
510 520 530 540 550
KFPENNLSQL TEQEINSLWS FDQASAKYQF EKYVRDYTGG SLSEDNGVDF
560 570 580 590 600
NKNTALDKNY LLNNKIPSNN VEEAGSKNYV HYIIQLQGDD ISYEATCNLF
610 620 630 640 650
SKNPKNSIII QRNMNESAKS YFLSDDGESI LELNKYRIPE RLKNKEKVKV
660 670 680 690 700
TFIGHGKDEF NTSEFARLSV DSLSNEISSF LDTIKLDISP KNVEVNLLGC
710 720 730 740 750
NMFSYDFNVE ETYPGKLLLS IMDKITSTLP DVNKNSITIG ANQYEVRINS
760 770 780 790 800
EGRKELLAHS GKWINKEEAI MSDLSSKEYI FFDSIDNKLK AKSKNIPGLA
810 820 830 840 850
SISEDIKTLL LDASVSPDTK FILNNLKLNI ESSIGDYIYY EKLEPVKNII
860 870 880 890 900
HNSIDDLIDE FNLLENVSDE LYELKKLNNL DEKYLISFED ISKNNSTYSV
910 920 930 940 950
RFINKSNGES VYVETEKEIF SKYSEHITKE ISTIKNSIIT DVNGNLLDNI
960 970 980 990 1000
QLDHTSQVNT LNAAFFIQSL IDYSSNKDVL NDLSTSVKVQ LYAQLFSTGL
1010 1020 1030 1040 1050
NTIYDSIQLV NLISNAVNDT INVLPTITEG IPIVSTILDG INLGAAIKEL
1060 1070 1080 1090 1100
LDEHDPLLKK ELEAKVGVLA INMSLSIAAT VASIVGIGAE VTIFLLPIAG
1110 1120 1130 1140 1150
ISAGIPSLVN NELILHDKAT SVVNYFNHLS ESKKYGPLKT EDDKILVPID
1160 1170 1180 1190 1200
DLVISEIDFN NNSIKLGTCN ILAMEGGSGH TVTGNIDHFF SSPSISSHIP
1210 1220 1230 1240 1250
SLSIYSAIGI ETENLDFSKK IMMLPNAPSR VFWWETGAVP GLRSLENDGT
1260 1270 1280 1290 1300
RLLDSIRDLY PGKFYWRFYA FFDYAITTLK PVYEDTNIKI KLDKDTRNFI
1310 1320 1330 1340 1350
MPTITTNEIR NKLSYSFDGA GGTYSLLLSS YPISTNINLS KDDLWIFNID
1360 1370 1380 1390 1400
NEVREISIEN GTIKKGKLIK DVLSKIDINK NKLIIGNQTI DFSGDIDNKD
1410 1420 1430 1440 1450
RYIFLTCELD DKISLIIEIN LVAKSYSLLL SGDKNYLISN LSNTIEKINT
1460 1470 1480 1490 1500
LGLDSKNIAY NYTDESNNKY FGAISKTSQK SIIHYKKDSK NILEFYNDST
1510 1520 1530 1540 1550
LEFNSKDFIA EDINVFMKDD INTITGKYYV DNNTDKSIDF SISLVSKNQV
1560 1570 1580 1590 1600
KVNGLYLNES VYSSYLDFVK NSDGHHNTSN FMNLFLDNIS FWKLFGFENI
1610 1620 1630 1640 1650
NFVIDKYFTL VGKTNLGYVE FICDNNKNID IYFGEWKTSS SKSTIFSGNG
1660 1670 1680 1690 1700
RNVVVEPIYN PDTGEDISTS LDFSYEPLYG IDRYINKVLI APDLYTSLIN
1710 1720 1730 1740 1750
INTNYYSNEY YPEIIVLNPN TFHKKVNINL DSSSFEYKWS TEGSDFILVR
1760 1770 1780 1790 1800
YLEESNKKIL QKIRIKGILS NTQSFNKMSI DFKDIKKLSL GYIMSNFKSF
1810 1820 1830 1840 1850
NSENELDRDH LGFKIIDNKT YYYDEDSKLV KGLININNSL FYFDPIEFNL
1860 1870 1880 1890 1900
VTGWQTINGK KYYFDINTGA ALTSYKIING KHFYFNNDGV MQLGVFKGPD
1910 1920 1930 1940 1950
GFEYFAPANT QNNNIEGQAI VYQSKFLTLN GKKYYFDNNS KAVTGWRIIN
1960 1970 1980 1990 2000
NEKYYFNPNN AIAAVGLQVI DNNKYYFNPD TAIISKGWQT VNGSRYYFDT
2010 2020 2030 2040 2050
DTAIAFNGYK TIDGKHFYFD SDCVVKIGVF STSNGFEYFA PANTYNNNIE
2060 2070 2080 2090 2100
GQAIVYQSKF LTLNGKKYYF DNNSKAVTGL QTIDSKKYYF NTNTAEAATG
2110 2120 2130 2140 2150
WQTIDGKKYY FNTNTAEAAT GWQTIDGKKY YFNTNTAIAS TGYTIINGKH
2160 2170 2180 2190 2200
FYFNTDGIMQ IGVFKGPNGF EYFAPANTDA NNIEGQAILY QNEFLTLNGK
2210 2220 2230 2240 2250
KYYFGSDSKA VTGWRIINNK KYYFNPNNAI AAIHLCTINN DKYYFSYDGI
2260 2270 2280 2290 2300
LQNGYITIER NNFYFDANNE SKMVTGVFKG PNGFEYFAPA NTHNNNIEGQ
2310 2320 2330 2340 2350
AIVYQNKFLT LNGKKYYFDN DSKAVTGWQT IDGKKYYFNL NTAEAATGWQ
2360 2370 2380 2390 2400
TIDGKKYYFN LNTAEAATGW QTIDGKKYYF NTNTFIASTG YTSINGKHFY
2410 2420 2430 2440 2450
FNTDGIMQIG VFKGPNGFEY FAPANTDANN IEGQAILYQN KFLTLNGKKY
2460 2470 2480 2490 2500
YFGSDSKAVT GLRTIDGKKY YFNTNTAVAV TGWQTINGKK YYFNTNTSIA
2510 2520 2530 2540 2550
STGYTIISGK HFYFNTDGIM QIGVFKGPDG FEYFAPANTD ANNIEGQAIR
2560 2570 2580 2590 2600
YQNRFLYLHD NIYYFGNNSK AATGWVTIDG NRYYFEPNTA MGANGYKTID
2610 2620 2630 2640 2650
NKNFYFRNGL PQIGVFKGSN GFEYFAPANT DANNIEGQAI RYQNRFLHLL
2660 2670 2680 2690 2700
GKIYYFGNNS KAVTGWQTIN GKVYYFMPDT AMAAAGGLFE IDGVIYFFGV
2710
DGVKAPGIYG
Length:2,710
Mass (Da):308,056
Last modified:February 1, 1996 - v2
Checksum:i0A6E52CE84C14421
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51797 Genomic DNA. Translation: CAA36094.1.
M30307 Genomic DNA. Translation: AAA23283.1.
X92982 Genomic DNA. Translation: CAA63564.1.
PIRiA37052.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X51797 Genomic DNA. Translation: CAA36094.1 .
M30307 Genomic DNA. Translation: AAA23283.1 .
X92982 Genomic DNA. Translation: CAA63564.1 .
PIRi A37052.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2F6E X-ray 1.85 A 2583-2709 [» ]
2G7C X-ray 2.00 A/B 2456-2710 [» ]
2QJ6 X-ray 2.50 A/B 2387-2706 [» ]
3HO6 X-ray 1.60 A/B 543-809 [» ]
4DMV X-ray 1.50 A 1-541 [» ]
4DMW X-ray 2.50 A 1-541 [» ]
ProteinModelPortali P16154.
SMRi P16154. Positions 1-542, 1862-1980, 2254-2706.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

CAZyi GT44. Glycosyltransferase Family 44.
MEROPSi C80.002.
TCDBi 1.C.57.1.2. the clostridial cytotoxin (cct) family.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P16154.

Family and domain databases

InterProi IPR018337. Cell_wall/Cho-bd_repeat.
IPR029044. Nucleotide-diphossugar_trans.
IPR020974. Pept_C80_RTX.
IPR024770. TcdA/TcdB_cat.
IPR024772. TcdA/TcdB_N.
IPR024769. TcdA/TcdB_pore_forming.
[Graphical view ]
Pfami PF01473. CW_binding_1. 12 hits.
PF11713. Peptidase_C80. 1 hit.
PF12919. TcdA_TcdB. 1 hit.
PF12920. TcdA_TcdB_pore. 1 hit.
PF12918. TcdB_N. 1 hit.
[Graphical view ]
SUPFAMi SSF53448. SSF53448. 1 hit.
PROSITEi PS51170. CW. 32 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Nucleotide sequence of Clostridium difficile toxin A."
    Sauerborn M., von Eichel-Streiber C.
    Nucleic Acids Res. 18:1629-1630(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 4325 / VPI 10463.
  2. "Molecular characterization of the Clostridium difficile toxin A gene."
    Dove C.H., Wang S.-Z., Price S.B., Phelps C.J., Lyerly D.M., Wilkins T.D., Johnson J.L.
    Infect. Immun. 58:480-488(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 4325 / VPI 10463.
  3. von Eichel-Streiber C.
    Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 4325 / VPI 10463.

Entry informationi

Entry nameiTOXA_PEPDI
AccessioniPrimary (citable) accession number: P16154
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: February 1, 1996
Last modified: November 26, 2014
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3