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Protein

Toxin B

Gene

toxB

Organism
Clostridioides difficile (Peptoclostridium difficile)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Cytotoxin.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei653PROSITE-ProRule annotation1
Active sitei698NucleophilePROSITE-ProRule annotation1

GO - Molecular functioni

  • cysteine-type peptidase activity Source: UniProtKB-KW
  • glucosyltransferase activity Source: UniProtKB

GO - Biological processi

  • pathogenesis Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Thiol protease, Toxin

Enzyme and pathway databases

BRENDAi2.4.1.B62. 13625.

Protein family/group databases

CAZyiGT44. Glycosyltransferase Family 44.
MEROPSiC80.003.
TCDBi1.C.57.1.1. the clostridial cytotoxin (cct) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Toxin B (EC:3.4.22.-)
Gene namesi
Name:toxB
Synonyms:tcdB
OrganismiClostridioides difficile (Peptoclostridium difficile)
Taxonomic identifieri1496 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptostreptococcaceaeClostridioides

Subcellular locationi

GO - Cellular componenti

  • host cell plasma membrane Source: AgBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000726362 – 2366Toxin BAdd BLAST2365

Proteomic databases

PRIDEiP18177.

Interactioni

Protein-protein interaction databases

IntActiP18177. 3 interactors.
MINTiMINT-2634250.
STRINGi272563.CD0660.

Structurei

Secondary structure

12366
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 12Combined sources7
Helixi22 – 34Combined sources13
Helixi42 – 62Combined sources21
Turni63 – 65Combined sources3
Helixi69 – 89Combined sources21
Beta strandi96 – 101Combined sources6
Helixi109 – 121Combined sources13
Beta strandi125 – 131Combined sources7
Helixi138 – 157Combined sources20
Helixi158 – 161Combined sources4
Beta strandi163 – 165Combined sources3
Helixi168 – 196Combined sources29
Helixi202 – 214Combined sources13
Helixi218 – 233Combined sources16
Turni234 – 236Combined sources3
Beta strandi237 – 239Combined sources3
Helixi240 – 242Combined sources3
Helixi244 – 247Combined sources4
Helixi252 – 260Combined sources9
Helixi265 – 280Combined sources16
Beta strandi282 – 285Combined sources4
Turni295 – 300Combined sources6
Helixi309 – 324Combined sources16
Helixi335 – 337Combined sources3
Helixi340 – 351Combined sources12
Helixi356 – 358Combined sources3
Beta strandi374 – 378Combined sources5
Beta strandi381 – 389Combined sources9
Helixi394 – 419Combined sources26
Helixi424 – 438Combined sources15
Turni441 – 443Combined sources3
Helixi444 – 450Combined sources7
Helixi451 – 455Combined sources5
Turni456 – 458Combined sources3
Helixi465 – 468Combined sources4
Helixi471 – 483Combined sources13
Helixi495 – 498Combined sources4
Helixi499 – 501Combined sources3
Helixi505 – 507Combined sources3
Helixi514 – 516Combined sources3
Helixi524 – 540Combined sources17
Beta strandi1835 – 1838Combined sources4
Beta strandi1841 – 1846Combined sources6
Turni1847 – 1850Combined sources4
Beta strandi1855 – 1859Combined sources5
Beta strandi1862 – 1867Combined sources6
Turni1868 – 1872Combined sources5
Beta strandi1877 – 1881Combined sources5
Beta strandi1884 – 1888Combined sources5
Beta strandi1897 – 1900Combined sources4
Beta strandi1902 – 1909Combined sources8
Beta strandi1927 – 1931Combined sources5
Beta strandi1934 – 1939Combined sources6
Turni1940 – 1942Combined sources3
Beta strandi1947 – 1951Combined sources5
Beta strandi1954 – 1958Combined sources5
Turni1960 – 1962Combined sources3
Beta strandi1968 – 1972Combined sources5
Beta strandi1975 – 1979Combined sources5
Beta strandi1988 – 1992Combined sources5
Beta strandi1995 – 1999Combined sources5
Beta strandi2008 – 2012Combined sources5
Beta strandi2015 – 2019Combined sources5
Beta strandi2028 – 2032Combined sources5
Beta strandi2035 – 2040Combined sources6
Turni2044 – 2046Combined sources3
Beta strandi2058 – 2062Combined sources5
Beta strandi2065 – 2069Combined sources5
Beta strandi2073 – 2075Combined sources3
Beta strandi2078 – 2081Combined sources4
Beta strandi2087 – 2090Combined sources4
Turni2092 – 2094Combined sources3
Beta strandi2097 – 2099Combined sources3
Beta strandi2254 – 2258Combined sources5
Beta strandi2261 – 2265Combined sources5
Beta strandi2274 – 2278Combined sources5
Beta strandi2281 – 2285Combined sources5
Beta strandi2294 – 2298Combined sources5
Beta strandi2301 – 2305Combined sources5
Beta strandi2324 – 2328Combined sources5
Beta strandi2331 – 2335Combined sources5
Beta strandi2339 – 2341Combined sources3
Beta strandi2344 – 2348Combined sources5
Beta strandi2351 – 2355Combined sources5
Turni2357 – 2359Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BVLX-ray2.20A2-541[»]
2BVMX-ray2.55A2-542[»]
4NC2X-ray2.50A2248-2366[»]
4NP4X-ray2.89A1834-2099[»]
ProteinModelPortaliP18177.
SMRiP18177.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18177.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini567 – 774Peptidase C80PROSITE-ProRule annotationAdd BLAST208
Repeati1832 – 1851Cell wall-binding 1Add BLAST20
Repeati1853 – 1872Cell wall-binding 2Add BLAST20
Repeati1875 – 1894Cell wall-binding 3Add BLAST20
Repeati1925 – 1944Cell wall-binding 4Add BLAST20
Repeati1966 – 1985Cell wall-binding 5Add BLAST20
Repeati1986 – 2005Cell wall-binding 6Add BLAST20
Repeati2006 – 2025Cell wall-binding 7Add BLAST20
Repeati2056 – 2075Cell wall-binding 8Add BLAST20
Repeati2076 – 2096Cell wall-binding 9Add BLAST21
Repeati2098 – 2117Cell wall-binding 10Add BLAST20
Repeati2118 – 2137Cell wall-binding 11Add BLAST20
Repeati2138 – 2157Cell wall-binding 12Add BLAST20
Repeati2208 – 2230Cell wall-binding 13Add BLAST23
Repeati2232 – 2251Cell wall-binding 14Add BLAST20
Repeati2252 – 2271Cell wall-binding 15Add BLAST20
Repeati2272 – 2291Cell wall-binding 16Add BLAST20
Repeati2322 – 2341Cell wall-binding 17Add BLAST20
Repeati2342 – 2361Cell wall-binding 18Add BLAST20

Sequence similaritiesi

Contains 18 cell wall-binding repeats.PROSITE-ProRule annotation
Contains 1 peptidase C80 domain.PROSITE-ProRule annotationCurated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4108N67. Bacteria.
COG5263. LUCA.

Family and domain databases

InterProiIPR018337. Cell_wall/Cho-bd_repeat.
IPR020974. CPD_dom.
IPR029044. Nucleotide-diphossugar_trans.
IPR024770. TcdA/TcdB_cat.
IPR024772. TcdA/TcdB_N.
IPR024769. TcdA/TcdB_pore_forming.
[Graphical view]
PfamiPF01473. CW_binding_1. 4 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.
PROSITEiPS51771. CGT_MARTX_CPD. 1 hit.
PS51170. CW. 18 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P18177-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLVNRKQLE KMANVRFRTQ EDEYVAILDA LEEYHNMSEN TVVEKYLKLK
60 70 80 90 100
DINSLTDIYI DTYKKSGRNK ALKKFKEYLV TEVLELKNNN LTPVEKNLHF
110 120 130 140 150
VWIGGQINDT AINYINQWKD VNSDYNVNVF YDSNAFLINT LKKTVVESAI
160 170 180 190 200
NDTLESFREN LNDPRFDYNK FFRKRMEIIY DKQKNFINYY KAQREENPEL
210 220 230 240 250
IIDDIVKTYL SNEYSKEIDE LNTYIEESLN KITQNSGNDV RNFEEFKNGE
260 270 280 290 300
SFNLYEQELV ERWNLAAASD ILRISALKEI GGMYLDVDML PGIQPDLFES
310 320 330 340 350
IEKPSSVTVD FWEMTKLEAI MKYKEYIPEY TSEHFDMLDE EVQSSFESVL
360 370 380 390 400
ASKSDKSEIF SSLGDMEASP LEVKIAFNSK GIINQGLISV KDSYCSNLIV
410 420 430 440 450
KQIENRYKIL NNSLNPAISE DNDFNTTTNT FIDSIMAEAN ADNGRFMMEL
460 470 480 490 500
GKYLRVGFFP DVKTTINLSG PEAYAAAYQD LLMFKEGSMN IHLIEADLRN
510 520 530 540 550
FEISKTNISQ STEQEMASLW SFDDARAKAQ FEEYKRNYFE GSLGEDDNLD
560 570 580 590 600
FSQNIVVDKE YLLEKISSLA RSSERGYIHY IVQLQGDKIS YEAACNLFAK
610 620 630 640 650
TPYDSVLFQK NIEDSEIAYY YNPGDGEIQE IDKYKIPSII SDRPKIKLTF
660 670 680 690 700
IGHGKDEFNT DIFAGFDVDS LSTEIEAAID LAKEDISPKS IEINLLGCNM
710 720 730 740 750
FSYSINVEET YPGKLLLKVK DKISELMPSI SQDSIIVSAN QYEVRINSEG
760 770 780 790 800
RRELLDHSGE WINKEESIIK DISSKEYISF NPKENKITVK SKNLPELSTL
810 820 830 840 850
LQEIRNNSNS SDIELEEKVM LTECEINVIS NIDTQIVEER IEEAKNLTSD
860 870 880 890 900
SINYIKDEFK LIESISDALC DLKQQNELED SHFISFEDIS ETDEGFSIRF
910 920 930 940 950
INKETGESIF VETEKTIFSE YANHITEEIS KIKGTIFDTV NGKLVKKVNL
960 970 980 990 1000
DTTHEVNTLN AAFFIQSLIE YNSSKESLSN LSVAMKVQVY AQLFSTGLNT
1010 1020 1030 1040 1050
ITDAAKVVEL VSTALDETID LLPTLSEGLP IIATIIDGVS LGAAIKELSE
1060 1070 1080 1090 1100
TSDPLLRQEI EAKIGIMAVN LTTATTAIIT SSLGIASGFS ILLVPLAGIS
1110 1120 1130 1140 1150
AGIPSLVNNE LVLRDKATKV VDYFKHVSLV ETEGVFTLLD DKIMMPQDDL
1160 1170 1180 1190 1200
VISEIDFNNN SIVLGKCEIW RMEGGSGHTV TDDIDHFFSA PSITYREPHL
1210 1220 1230 1240 1250
SIYDVLEVQK EELDLSKDLM VLPNAPNRVF AWETGWTPGL RSLENDGTKL
1260 1270 1280 1290 1300
LDRIRDNYEG EFYWRYFAFI ADALITTLKP RYEDTNIRIN LDSNTRSFIV
1310 1320 1330 1340 1350
PIITTEYIRE KLSYSFYGSG GTYALSLSQY NMGINIELSE SDVWIIDVDN
1360 1370 1380 1390 1400
VVRDVTIESD KIKKGDLIEG ILSTLSIEEN KIILNSHEIN FSGEVNGSNG
1410 1420 1430 1440 1450
FVSLTFSILE GINAIIEVDL LSKSYKLLIS GELKILMLNS NHIQQKIDYI
1460 1470 1480 1490 1500
GFNSELQKNI PYSFVDSEGK ENGFINGSTK EGLFVSELPD VVLISKVYMD
1510 1520 1530 1540 1550
DSKPSFGYYS NNLKDVKVIT KDNVNILTGY YLKDDIKISL SLTLQDEKTI
1560 1570 1580 1590 1600
KLNSVHLDES GVAEILKFMN RKGNTNTSDS LMSFLESMNI KSIFVNFLQS
1610 1620 1630 1640 1650
NIKFILDANF IISGTTSIGQ FEFICDENDN IQPYFIKFNT LETNYTLYVG
1660 1670 1680 1690 1700
NRQNMIVEPN YDLDDSGDIS STVINFSQKY LYGIDSCVNK VVISPNIYTD
1710 1720 1730 1740 1750
EINITPVYET NNTYPEVIVL DANYINEKIN VNINDLSIRY VWSNDGNDFI
1760 1770 1780 1790 1800
LMSTSEENKV SQVKIRFVNV FKDKTLANKL SFNFSDKQDV PVSEIILSFT
1810 1820 1830 1840 1850
PSYYEDGLIG YDLGLVSLYN EKFYINNFGM MVSGLIYIND SLYYFKPPVN
1860 1870 1880 1890 1900
NLITGFVTVG DDKYYFNPIN GGAASIGETI IDDKNYYFNQ SGVLQTGVFS
1910 1920 1930 1940 1950
TEDGFKYFAP ANTLDENLEG EAIDFTGKLI IDENIYYFDD NYRGAVEWKE
1960 1970 1980 1990 2000
LDGEMHYFSP ETGKAFKGLN QIGDYKYYFN SDGVMQKGFV SINDNKHYFD
2010 2020 2030 2040 2050
DSGVMKVGYT EIDGKHFYFA ENGEMQIGVF NTEDGFKYFA HHNEDLGNEE
2060 2070 2080 2090 2100
GEEISYSGIL NFNNKIYYFD DSFTAVVGWK DLEDGSKYYF DEDTAEAYIG
2110 2120 2130 2140 2150
LSLINDGQYY FNDDGIMQVG FVTINDKVFY FSDSGIIESG VQNIDDNYFY
2160 2170 2180 2190 2200
IDDNGIVQIG VFDTSDGYKY FAPANTVNDN IYGQAVEYSG LVRVGEDVYY
2210 2220 2230 2240 2250
FGETYTIETG WIYDMENESD KYYFNPETKK ACKGINLIDD IKYYFDEKGI
2260 2270 2280 2290 2300
MRTGLISFEN NNYYFNENGE MQFGYINIED KMFYFGEDGV MQIGVFNTPD
2310 2320 2330 2340 2350
GFKYFAHQNT LDENFEGESI NYTGWLDLDE KRYYFTDEYI AATGSVIIDG
2360
EEYYFDPDTA QLVISE
Length:2,366
Mass (Da):269,712
Last modified:January 23, 2007 - v3
Checksum:iE1024BD8B8A56ADF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53138 Genomic DNA. Translation: CAA37298.1.
X92982 Genomic DNA. Translation: CAA63562.1.
X60984 Genomic DNA. Translation: CAA43299.1.
PIRiA27636.
S10317.
RefSeqiWP_009902069.1. NZ_LN831031.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X53138 Genomic DNA. Translation: CAA37298.1.
X92982 Genomic DNA. Translation: CAA63562.1.
X60984 Genomic DNA. Translation: CAA43299.1.
PIRiA27636.
S10317.
RefSeqiWP_009902069.1. NZ_LN831031.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BVLX-ray2.20A2-541[»]
2BVMX-ray2.55A2-542[»]
4NC2X-ray2.50A2248-2366[»]
4NP4X-ray2.89A1834-2099[»]
ProteinModelPortaliP18177.
SMRiP18177.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP18177. 3 interactors.
MINTiMINT-2634250.
STRINGi272563.CD0660.

Protein family/group databases

CAZyiGT44. Glycosyltransferase Family 44.
MEROPSiC80.003.
TCDBi1.C.57.1.1. the clostridial cytotoxin (cct) family.

Proteomic databases

PRIDEiP18177.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108N67. Bacteria.
COG5263. LUCA.

Enzyme and pathway databases

BRENDAi2.4.1.B62. 13625.

Miscellaneous databases

EvolutionaryTraceiP18177.

Family and domain databases

InterProiIPR018337. Cell_wall/Cho-bd_repeat.
IPR020974. CPD_dom.
IPR029044. Nucleotide-diphossugar_trans.
IPR024770. TcdA/TcdB_cat.
IPR024772. TcdA/TcdB_N.
IPR024769. TcdA/TcdB_pore_forming.
[Graphical view]
PfamiPF01473. CW_binding_1. 4 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.
PROSITEiPS51771. CGT_MARTX_CPD. 1 hit.
PS51170. CW. 18 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTOXB_CLODI
AccessioniPrimary (citable) accession number: P18177
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 103 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.