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Protein

Adenosine monophosphate-protein transferase and cysteine protease IbpA

Gene

ibpA

Organism
Histophilus somni (strain 2336) (Haemophilus somnus)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adenylyltransferase involved in virulence by mediating the addition of adenosine 5'-monophosphate (AMP) to specific tyrosine residue of host Rho GTPases RhoA, Rac and Cdc42. The resulting AMPylation inactivates Rho GTPases, thereby inhibiting actin assembly in infected cells. Probably also acts as a cysteine protease, which may play a central role after invasion of host cell and in virulence. Possible member (with IbpB) of a 2 partner secretion. Probably able to bind bovine epithelial cells (host cells). May participate in the formation of fibrils at the surface of the bacteria.4 Publications

Catalytic activityi

ATP + [protein] = diphosphate + [protein]-AMP.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei3728ATP1
Binding sitei3757ATP1
Active sitei3910For cysteine protease activitySequence analysis1
Active sitei4033For cysteine protease activitySequence analysis1
Active sitei4048For cysteine protease activitySequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi3670 – 3671ATP2
Nucleotide bindingi3722 – 3724ATP3

GO - Molecular functioni

GO - Biological processi

  • cellular protein modification process Source: UniProtKB
  • negative regulation of GTPase activity Source: UniProtKB
  • pathogenesis Source: UniProtKB
  • protein adenylylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Nucleotidyltransferase, Protease, Thiol protease, Transferase

Keywords - Biological processi

Virulence

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Adenosine monophosphate-protein transferase and cysteine protease IbpA
Short name:
HMW IgBP
Alternative name(s):
p120
Cleaved into the following chain:
Alternative name(s):
76 kDa antigen
Including the following 2 domains:
Adenosine monophosphate-protein transferase IbpA (EC:2.7.7.n1)
Alternative name(s):
AMPylator IbpA
Cysteine protease IbpA (EC:3.4.22.-)
Gene namesi
Name:ibpA
Synonyms:p76
Ordered Locus Names:HSM_1489
OrganismiHistophilus somni (strain 2336) (Haemophilus somnus)
Taxonomic identifieri228400 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus
Proteomesi
  • UP000008543 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell outer membrane, Membrane, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi3535 – 3536IP → AA: Reduced adenylyltransferase toward Rho GTPase family proteins. 1 Publication2
Mutagenesisi3552 – 3553IL → AA: Reduced adenylyltransferase toward Rho GTPase family proteins. 1 Publication2
Mutagenesisi3668 – 3670LTK → ATA: Reduced adenylyltransferase activity. 1 Publication3
Mutagenesisi3717H → A: Abolishes adenylyltransferase activity. 2 Publications1
Mutagenesisi3723N → A: Does not affect adenylyltransferase activity. 1 Publication1
Mutagenesisi3724G → A: Nucleotide-binding mutant. No adenylyltransferase activity abd reduced toxicity. 1 Publication1
Mutagenesisi3725R → A: Does not affect adenylyltransferase activity. 1 Publication1
Mutagenesisi3728R → A: Does not affect adenylyltransferase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 97Sequence analysisAdd BLAST97
ChainiPRO_000033840898 – 4095Adenosine monophosphate-protein transferase and cysteine protease IbpAAdd BLAST3998
ChainiPRO_00001925103222 – 4095Protein p76 IgBPAdd BLAST874

Post-translational modificationi

The long form of the protein is probably processed, and/or the transcript may be subject to differential translational initiation.

Proteomic databases

PRIDEiQ06277.

Interactioni

Subunit structurei

Immunoglobulin-binding protein.1 Publication

Structurei

Secondary structure

14095
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3499 – 3511Combined sources13
Helixi3513 – 3516Combined sources4
Turni3517 – 3519Combined sources3
Helixi3521 – 3534Combined sources14
Helixi3539 – 3543Combined sources5
Helixi3549 – 3552Combined sources4
Helixi3555 – 3568Combined sources14
Helixi3574 – 3585Combined sources12
Helixi3596 – 3609Combined sources14
Helixi3612 – 3616Combined sources5
Helixi3618 – 3635Combined sources18
Helixi3642 – 3651Combined sources10
Beta strandi3668 – 3670Combined sources3
Helixi3678 – 3697Combined sources20
Helixi3702 – 3716Combined sources15
Beta strandi3719 – 3721Combined sources3
Helixi3723 – 3737Combined sources15
Turni3748 – 3750Combined sources3
Helixi3751 – 3754Combined sources4
Beta strandi3758 – 3762Combined sources5
Helixi3767 – 3779Combined sources13
Turni3780 – 3782Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3N3UX-ray1.85A3488-3786[»]
4ITRX-ray2.30A/B3482-3797[»]
ProteinModelPortaliQ06277.
SMRiQ06277.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06277.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati2250 – 22711Add BLAST22
Repeati2272 – 22952Add BLAST24
Repeati2296 – 23173Add BLAST22
Repeati2318 – 23434Add BLAST26
Repeati2344 – 23655Add BLAST22
Repeati2366 – 23876Add BLAST22
Repeati2388 – 24137Add BLAST26
Repeati2414 – 24358Add BLAST22
Repeati2436 – 24579Add BLAST22
Repeati2458 – 248310Add BLAST26
Repeati2484 – 250511Add BLAST22
Repeati2506 – 252712Add BLAST22
Domaini3218 – 3355Fido 1PROSITE-ProRule annotationAdd BLAST138
Domaini3640 – 3777Fido 2PROSITE-ProRule annotationAdd BLAST138

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni972 – 1515Binds bovine IgG2 FcAdd BLAST544
Regioni1116 – 1255Binds bovine IgG2 FcAdd BLAST140
Regioni2250 – 252712 X 22 AA approximate repeatsAdd BLAST278
Regioni3222 – 4095yopT-likeAdd BLAST874
Regioni3354 – 3698Binds bovine IgG2 FcAdd BLAST345
Regioni3535 – 3557Arm regionAdd BLAST23

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1116 – 1247Sequence analysisAdd BLAST132

Domaini

The fido domains mediate the adenylyltransferase activity.
The arm region dictates the ability to recognize Rho family proteins. Leu-3668 and Lys-3670 probably lock the position of Tyr substrate in the correct orientation for modification (PubMed:20622875).1 Publication
When associated with Cdc42 target, adopts a conformation that mimicks the GDI-bound state of Rho GTPases.1 Publication

Sequence similaritiesi

In the central section; belongs to the fic family.Curated
In the C-terminal section; belongs to the peptidase C58 family.Curated
Contains 2 fido domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, Signal

Phylogenomic databases

HOGENOMiHOG000112991.
KOiK15125.
OMAiVSPITDK.
OrthoDBiPOG091H023K.

Family and domain databases

Gene3Di1.10.3290.10. 2 hits.
2.160.20.10. 1 hit.
InterProiIPR024973. ESPR.
IPR003812. Fido.
IPR008638. Filamn_hemagglutn_N.
IPR025157. Haemagluttinin_rpt.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR003951. Peptidase_C58.
IPR006473. Peptidase_C58_Yopt.
[Graphical view]
PfamiPF13018. ESPR. 1 hit.
PF02661. Fic. 2 hits.
PF13332. Fil_haemagg_2. 1 hit.
PF05860. Haemagg_act. 1 hit.
PF03543. Peptidase_C58. 1 hit.
[Graphical view]
PRINTSiPR01376. BACSURFANTGN.
SMARTiSM00912. Haemagg_act. 1 hit.
[Graphical view]
SUPFAMiSSF140931. SSF140931. 2 hits.
SSF51126. SSF51126. 1 hit.
TIGRFAMsiTIGR01901. adhes_NPXG. 1 hit.
TIGR01586. yopT_cys_prot. 1 hit.
PROSITEiPS51459. FIDO. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q06277-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKNCYKLIF SKTRGCLVPV AECITSAVDS GSSDSVVVSE KTDEEDRQGS
60 70 80 90 100
IEDYRLSNVC LSVKTFLNPV SSALCLNWKS VSVLLLSMVA APNFAQSAEE
110 120 130 140 150
AAKAEKTPKL TEIQNGNDGI QLETKNQNIG VGAGTTENNH PTKLYKTENN
160 170 180 190 200
VIVIDIAKPN DKGISDNRFQ KFNIPNGAVF KNNKDQQRSE LVGYLEGNKN
210 220 230 240 250
LADKEAKVIL NQVTGSELSQ IKGALEILGT KADLVIANQH GINLNGVQTI
260 270 280 290 300
NAGRFVATTS KLIDPNKMEF DVTQGTVTID VNGFATDNLP YLDIVAKKIE
310 320 330 340 350
QKGTIGNKEK EKNKTSETEI TFIAGKGKIK YNIENDGKTK LEVQKDSNTS
360 370 380 390 400
QPSDKEEVAI TGASTGAMHG KSIKLIVTEQ GAGVKHDGII LSENDIKIES
410 420 430 440 450
NKGDIDLGDK LQAKNEISLN NAKRITIANE ITADKSITIT ADDVKLKNNK
460 470 480 490 500
EASATEEAKL KGKGKLASKK VKVEAKKSLV LDDETKVVAT DLELKSQTLT
510 520 530 540 550
NQGRIYGNKV KIDTDKLVNK KEIYAEDNLD ITTKGKTVTV SVNKDNKRKA
560 570 580 590 600
DVKEETVADL DVGFENTGTI ESKSKAKLTF KDNTSFVSKG NKFIKAKDEL
610 620 630 640 650
TIDAQNVVIS ENDELQTTAR LTINAAGNVV NNGLLASGKT LTINAKQGSI
660 670 680 690 700
YNEKGILGAR EQLTLSAKGN NKETEGNIIN GADSLLHSEG KMELDAENTV
710 720 730 740 750
YNLGNIFAKS DLTVKANELI NDVKLSGSIT KKSPYSVLNR YRRSDIASHG
760 770 780 790 800
WHNNDYRLWI NPIEFEKAEV KVEKAGLIRA EGNFKFEGKK GDNQQDATLT
810 820 830 840 850
NHGVINVKNT FEAQNAKVVN NMKAYQANLL TEFFKQKQDI TFNYQPRARL
860 870 880 890 900
FLSALSGQAE RKFNSLEELF DGLFSEQPIT NSSSYYADNS QAVHLLEEIK
910 920 930 940 950
SPTFQKAMTL VFGANWKNED HKKLSQRWKE FKEKQDAHFD YRPTDKAKIL
960 970 980 990 1000
AQRINGKIDE LKNGSTGGFS ESERITVGQH KFDLSKVEFR SEVNRKENLN
1010 1020 1030 1040 1050
NSNVDLSALS DLLSIPNLFV DNSVQLDKTV DKNIEIDEED EFLLKPHTGE
1060 1070 1080 1090 1100
EPDLLNENEL SENGKFLDKL LGEIGEKTYI REVSDDWERD PDEPDEPDYK
1110 1120 1130 1140 1150
TESRLETRDR FDTLPSEVQD KLRQKFNEYK EKAQQKRQAE ALQAKTKNEQ
1160 1170 1180 1190 1200
LQSDLETGYK EEEKRQAKND LEKQAELQQL DQQEKEKLAK EKELQGKINE
1210 1220 1230 1240 1250
EKQQEALAKQ KQEQQKQADA KAKIEEEKRL EEYRKELAKD HQIEEALSKN
1260 1270 1280 1290 1300
QFLKEVDDTR PKVETDPLYR TKLQYINQDE YFGSKYFLNK VGSSTDAGKK
1310 1320 1330 1340 1350
VAVIGDNYLE HQLITKSIEK KVDNHLALKY QVNDAQLVKK LIDNSYFESK
1360 1370 1380 1390 1400
ELGLKVGEAL TKEQQNQLKQ DIVWYVKANI NNKEVLLPQV YFANKTLRDA
1410 1420 1430 1440 1450
EKFKGLGDAL IRANEINLKT RDVLNSGTIS GKNIDIEAEN KIKNRGDILS
1460 1470 1480 1490 1500
EESTRLVGHK GIDNTARSFV NGNGDVEVQR ASIRTEGHLH LEADEDSDIN
1510 1520 1530 1540 1550
SKGSDIKGKT GFVKARNFNT TDTHRTEHSV EKGRIFSKKG EILGYRKEST
1560 1570 1580 1590 1600
QKAISVGSNT EFDHVHFAIK NDVNQEGSKI KAKVVTGVVQ GDYNTKAGRN
1610 1620 1630 1640 1650
AQQTERYIRL DQEYSSGHIS GAGFTVSHER DSQNGEKTNI GGASSNTGTG
1660 1670 1680 1690 1700
FTLGGSFSET REKETSLTHT NSDLQVDHGI LHVLKKAEIG GVDINKHKFT
1710 1720 1730 1740 1750
GKAVEEDEAK AEQQAKAKAA PDATDNAAQK EEPKFKVLSQ SEVDDLMTEK
1760 1770 1780 1790 1800
SANDLFNKYK KVKEDEGFEL SAKEITSNKQ KDEYHLDSER SVLKFGIETE
1810 1820 1830 1840 1850
GHSAIADAVS HVAKEIVEAQ RGVKQDGTVA LQHISDVANI VTGELVGGSS
1860 1870 1880 1890 1900
KFGFERNYET NKVKETSDIR TKIAGNITLS AHGGNLQLKN VESDANSKLT
1910 1920 1930 1940 1950
LQAKRNVDIL DGETTRESTE RQSRQKFAFG INSGCSVMSG GCNGGVSGSV
1960 1970 1980 1990 2000
DGNESFTTEK SVTHNNSLLR AKNLKIAAGK DLNLISSNIK ADHLDLNIKG
2010 2020 2030 2040 2050
KTNIVSKQDS FDRLYRGFDF SASAGAALSS STLVKGNGSF GAGYTHEVEN
2060 2070 2080 2090 2100
RKLLNQQAGI VANRITGQIK DLDLVAAHFI NKDENSGFRV SGNVTSQQLN
2110 2120 2130 2140 2150
DSHHKDGGSV GVSVGINERG ASSFNVRGGR AEQKHYDAVQ KSVISGINLK
2160 2170 2180 2190 2200
DNNVTGEIVD DLSKAKTVTR DDVYASTQFN FEVADLVELG EKAKSKLQSK
2210 2220 2230 2240 2250
FSKAVNNDAE QPTTTRISSE DVVEMVDNPL YGSNADVRKL RTLDEVGEGY
2260 2270 2280 2290 2300
STLGDQNANK GRKLPNGSDD IYSLLGKVKV SGDEPVYDKV SAEGAYDLLG
2310 2320 2330 2340 2350
DSNANKGRTL RNNSDDLYST VGDANSDISR IRSNVYDEIA AGPYSLLGRT
2360 2370 2380 2390 2400
KAAEEHIYEQ IGEGPYSLLG NGSAVRNRTL GGESNSTYST VGDANSDISR
2410 2420 2430 2440 2450
IRSNVYDEIV AGPYSLLGKP KAAEEHIYEQ IGEGPYSLLG NGSAVRNRTL
2460 2470 2480 2490 2500
GGESDSPYST VGDANSDISR IRSNVYDEIV AGPYSLLGRT KAAEEHIYEQ
2510 2520 2530 2540 2550
IGEGPYSLLG NGSAVRNRTL GGESDSPYSL LGGEGTRNKV LADTIESIYS
2560 2570 2580 2590 2600
TLSRPQASSN LEMVDNPLYD SVRRSASDQL PELPTVRNLL NSDTEAGNGT
2610 2620 2630 2640 2650
YSEITSRTRN ANDPLPPLPN EFRTRLSQGA DLADHVYDTI GSIYSVLSKP
2660 2670 2680 2690 2700
KASSNLEMVD NPLYGSVRRA AGDQLPELPT VKTLLNKVEE VGNEIYSEIT
2710 2720 2730 2740 2750
SKTRSANDPL PALPNFRLTQ EVDTADHIYA DINDVVNRAN KAKRDLPATP
2760 2770 2780 2790 2800
EATPKVAVDG GDYATIGEVS PLQPRASRQQ GSSDYEEIPL PQETAPQKTS
2810 2820 2830 2840 2850
PVKRTSAEGE DGYATIAEVL QPRAAKGQVS DYETIPLDEP SQAAVRTERS
2860 2870 2880 2890 2900
AVEGDYAEIT SPSIQPRSAR GQSGGEEFEP FPSEFSSEPQ SPKRALPAEN
2910 2920 2930 2940 2950
AVVNELGNEL KARLKSKEDQ ANPAKAEVSE PIYATLDKSP EGLARAKAKG
2960 2970 2980 2990 3000
DEAAAANPIV KTRVEDDVAP ELPARPSNLS DSISNETIAE NGQSVALGTP
3010 3020 3030 3040 3050
KSAVAESNRN NNGNQKLQSE GAEGVSPKTK SEDKSWFAKV KDFFFAKSNK
3060 3070 3080 3090 3100
SQAKEAKSEQ ETVSKPNYDS LEDDLNLKNL LALEDKRGSS FEENVLKNPE
3110 3120 3130 3140 3150
FLAEAREIAK KYIPEATIKQ MGNSPEFDEI LTEGAKKVEK RINDALTFKP
3160 3170 3180 3190 3200
SVDEFNEIQG LVKNIQKGSA VDDLNAQTLA ITEALADTSK TIQRNPKLKE
3210 3220 3230 3240 3250
EVQGAIEEFL KSSQGKELTV EMIEKLNHGL RPDEGSDRLL YKKENLTKEN
3260 3270 3280 3290 3300
AVFSSPQASK IQLNETVDFI NQAIKQNVEP SVLAGLVYQR LIAYHPFAEG
3310 3320 3330 3340 3350
NGRMARVVVN KILLDAGYPP FTKFSSEFET QIIPQTKATA KSATSAEVVK
3360 3370 3380 3390 3400
EFLTELGKKS SPQEGGANNQ NGQATSPVTL KSKDVSEVEN TQSADSLTIK
3410 3420 3430 3440 3450
QPEQGKAGGQ LPSVPKVETS VNEVAPLSSV PAELKDAAGG NKKAAEKSEG
3460 3470 3480 3490 3500
ATGVEKEKTT LFQRVKQFFT GSKSGAKPVA GDETANKVNY QDLEDNLNLK
3510 3520 3530 3540 3550
GLISLEDDRN ANFESNVLKN EKFLDEAREI SKKSIPEATV KQMSHLPEFD
3560 3570 3580 3590 3600
DILTEGAKKV ESRINKAITF RPSVEEFSEI QDLVKTLPKT KVIEDLSTKT
3610 3620 3630 3640 3650
NEITEALAAT SKTIQRTPEL KEQLKTAIED FLQNSQGKPL TVQMIENLNH
3660 3670 3680 3690 3700
GLRPDEGEGR LLYKKENLTK ENAVFSSPEA AKIQLAETVD FINRAKNEGI
3710 3720 3730 3740 3750
EPSVVGALVY QRLIAYHPFA EGNGRMARVI VNKILLDAGY PAFTKFSDEF
3760 3770 3780 3790 3800
EPQIIPQTKA STKSATSSEV VVEFLKELAK KGSKEDNEQN LEKTDRTSTD
3810 3820 3830 3840 3850
LTESAVENSA ALSSGTVRSA TVSETVTETE QAKAKPVSDL VSSKDLVEQQ
3860 3870 3880 3890 3900
RTVLQRIQDQ FQPLKVKSKI DAVRSSVEEF GGEVSFKFAQ SKGEVYKEIV
3910 3920 3930 3940 3950
KHIETQNGVC ESTCAHWIAK NVNPTDENFF NTLYEGGKKG HLKKETIDSI
3960 3970 3980 3990 4000
KKLQTEFINS GSATQQFKLT DSWLQEQGVV PKEKKVADFV RRDEVSGTVS
4010 4020 4030 4040 4050
KNDVSSLVKA ILDTGDDTAG VKKISINLEG GSHTVSAAVD GSKVTFFDPN
4060 4070 4080 4090
FGEMTFPTHQ QFENWLKNAF WQKSGYAGKQ EGRRFFNVVN YKKNN
Length:4,095
Mass (Da):450,060
Last modified:June 10, 2008 - v2
Checksum:i495723E626D5E7DD
GO

Sequence cautioni

The sequence AAC36827 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB087258 Genomic DNA. Translation: BAC78649.1.
L10282 Unassigned DNA. Translation: AAC36827.1. Different initiation.
CP000947 Genomic DNA. Translation: ACA31239.1.
RefSeqiWP_012340627.1. NC_010519.1.

Genome annotation databases

EnsemblBacteriaiACA31239; ACA31239; HSM_1489.
KEGGihsm:HSM_1489.
PATRICi20200200. VBIHaeSom93646_1569.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB087258 Genomic DNA. Translation: BAC78649.1.
L10282 Unassigned DNA. Translation: AAC36827.1. Different initiation.
CP000947 Genomic DNA. Translation: ACA31239.1.
RefSeqiWP_012340627.1. NC_010519.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3N3UX-ray1.85A3488-3786[»]
4ITRX-ray2.30A/B3482-3797[»]
ProteinModelPortaliQ06277.
SMRiQ06277.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ06277.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACA31239; ACA31239; HSM_1489.
KEGGihsm:HSM_1489.
PATRICi20200200. VBIHaeSom93646_1569.

Phylogenomic databases

HOGENOMiHOG000112991.
KOiK15125.
OMAiVSPITDK.
OrthoDBiPOG091H023K.

Miscellaneous databases

EvolutionaryTraceiQ06277.

Family and domain databases

Gene3Di1.10.3290.10. 2 hits.
2.160.20.10. 1 hit.
InterProiIPR024973. ESPR.
IPR003812. Fido.
IPR008638. Filamn_hemagglutn_N.
IPR025157. Haemagluttinin_rpt.
IPR012334. Pectin_lyas_fold.
IPR011050. Pectin_lyase_fold/virulence.
IPR003951. Peptidase_C58.
IPR006473. Peptidase_C58_Yopt.
[Graphical view]
PfamiPF13018. ESPR. 1 hit.
PF02661. Fic. 2 hits.
PF13332. Fil_haemagg_2. 1 hit.
PF05860. Haemagg_act. 1 hit.
PF03543. Peptidase_C58. 1 hit.
[Graphical view]
PRINTSiPR01376. BACSURFANTGN.
SMARTiSM00912. Haemagg_act. 1 hit.
[Graphical view]
SUPFAMiSSF140931. SSF140931. 2 hits.
SSF51126. SSF51126. 1 hit.
TIGRFAMsiTIGR01901. adhes_NPXG. 1 hit.
TIGR01586. yopT_cys_prot. 1 hit.
PROSITEiPS51459. FIDO. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiIBPA_HISS2
AccessioniPrimary (citable) accession number: Q06277
Secondary accession number(s): B0UUL0, Q7WZI3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 29, 2003
Last sequence update: June 10, 2008
Last modified: November 30, 2016
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

The reaction mechanisms probably follows a substrate-assisted attack of ATP. According to this model, His-3717 acts by attracting a proton from the Tyr substrate, thereby preparing the Tyr as a nucleophile to attack the alpha-phosphate of ATP. This model is consistent with the observation that hydrolysis of ATP is very slow in the absence of Rho GTPases (PubMed:20622875).1 Publication

Caution

Was originally [PubMed:8245839] thought to be a 76 kDa immunoglobulin-binding protein; it is now apparent that the gene is much longer but how it is translated and processed is unclear.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

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.