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Q4A127

- HSDR_STAS1

UniProt

Q4A127 - HSDR_STAS1

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Protein

Type-1 restriction enzyme R protein

Gene

hsdR

Organism
Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

Subunit R is required for both nuclease and ATPase activities, but not for modification.By similarity

Catalytic activityi

Endonucleolytic cleavage of DNA to give random double-stranded fragments with terminal 5'-phosphates; ATP is simultaneously hydrolyzed.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi268 – 2747ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: UniProtKB-KW
  3. Type I site-specific deoxyribonuclease activity Source: UniProtKB-EC

GO - Biological processi

  1. DNA restriction-modification system Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Restriction system

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciSSAP342451:GKFA-56-MONOMER.

Protein family/group databases

REBASEi11264. SsaAORF53P.

Names & Taxonomyi

Protein namesi
Recommended name:
Type-1 restriction enzyme R protein (EC:3.1.21.3)
Alternative name(s):
Type I restriction enzyme R protein
Gene namesi
Name:hsdR
Ordered Locus Names:SSP0054
OrganismiStaphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229)
Taxonomic identifieri342451 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000006371: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 930930Type-1 restriction enzyme R proteinPRO_0000077272Add
BLAST

Interactioni

Subunit structurei

The type I restriction/modification system is composed of three polypeptides R, M and S.By similarity

Protein-protein interaction databases

STRINGi342451.SSP0054.

Structurei

3D structure databases

ProteinModelPortaliQ4A127.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini254 – 418165Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the HsdR family.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0610.
HOGENOMiHOG000003518.
KOiK01153.
OMAiNNGYIWH.
OrthoDBiEOG6JTCB4.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR006935. Helicase/UvrB_dom.
IPR014001. Helicase_ATP-bd.
IPR027417. P-loop_NTPase.
IPR007409. Restrct_endonuc_type1_HsdR_N.
IPR004473. Restrct_endonuc_typeI_HsdR.
IPR022625. TypeI_RM_Rsu_C.
[Graphical view]
PfamiPF12008. EcoR124_C. 1 hit.
PF04313. HSDR_N. 1 hit.
PF04851. ResIII. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00348. hsdR. 1 hit.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q4A127-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MVYQSEFALE TEMMEQLKSN GYETVTIRNE QQLLDNFRSI LNERHADKLN
60 70 80 90 100
GDPLTDKEFQ RLLTMINGKG IFESARILRD KMPLKRDDES EVYLSFLDTR
110 120 130 140 150
HWCQNKFQIT NQVSVDDTYK ARYDVTILIN GLPLVQIELK RRGIDINEAF
160 170 180 190 200
NQVMRYRKQN YTGLFRYIQL FIISNGIDTR YISNNDGEIY KSHMFYWSDK
210 220 230 240 250
ENNRINTLNE FTETFLRPCH IAKMISRYMI LNETDNILMA MRPYQVHAVE
260 270 280 290 300
ALIHQATETS NNGYIWHTTG SGKTLTSFKA SQVLSEQDDI KKVIFLVDRK
310 320 330 340 350
DLDSQTEEEF NKFSKGSVDK TNNTAQLVKQ LKDKSLPLIV TTIQKMSKAI
360 370 380 390 400
QNNAEALDQY KTDKVVFIID ECHRSQFGDM HRIVRQHFNN AQYFGFTGTP
410 420 430 440 450
RFEENQSQDG RSTADIFGRC LHTYLIKDAI HDGNVLGFSV DYINTIKAQN
460 470 480 490 500
IDTETDELVE GINTDEVWLS DQRVELIARH ITENHDKYTR NRQYSAIFTV
510 520 530 540 550
QSIPALVKYY DAFKKISKDY EHPLKVAGVF SYAANEERNE GEVDEAHSRG
560 570 580 590 600
KLEEVIQDYN LNFGTNFSTD TFQEYFNHIS KNVKKGVKDN KIDVLIVVNM
610 620 630 640 650
FLTGFDSKVL NTLYVDKNLK YHDLIQAYSR TNRVEKETKP FGKIVNYRDL
660 670 680 690 700
KQNTDNALKL FSQTEDTDRV LMRDYDEYKA EFVDALAELK AVALKPQDMD
710 720 730 740 750
QVQDENEKKA FVEAFRLVSK LVLRLKAFDE FDFTKANIGM NEQEFEDYKS
760 770 780 790 800
KYFAIYDEVK PKRGEVEKVS ILNDIDFEIE ILRNDRINVS YIMDLVRQID
810 820 830 840 850
LKDKAEQQRN RDQIRRMLDN ADDPTLRLKR DLLREFIDDV IPELSEEDNI
860 870 880 890 900
DEAYILFENA KRESEFNQFA QQQAVDEQVL KDITGEYEYS GIVNQDHLKE
910 920 930
LVGDKKLREK RQTKKAVTSF VEEVSEKYSS
Length:930
Mass (Da):108,873
Last modified:September 13, 2005 - v1
Checksum:i559FA69A2AC96E24
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008934 Genomic DNA. Translation: BAE17199.1.
RefSeqiYP_300144.1. NC_007350.1.

Genome annotation databases

EnsemblBacteriaiBAE17199; BAE17199; SSP0054.
GeneIDi3617259.
KEGGissp:SSP0054.
PATRICi19621587. VBIStaSap90642_0054.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008934 Genomic DNA. Translation: BAE17199.1 .
RefSeqi YP_300144.1. NC_007350.1.

3D structure databases

ProteinModelPortali Q4A127.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 342451.SSP0054.

Protein family/group databases

REBASEi 11264. SsaAORF53P.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAE17199 ; BAE17199 ; SSP0054 .
GeneIDi 3617259.
KEGGi ssp:SSP0054.
PATRICi 19621587. VBIStaSap90642_0054.

Phylogenomic databases

eggNOGi COG0610.
HOGENOMi HOG000003518.
KOi K01153.
OMAi NNGYIWH.
OrthoDBi EOG6JTCB4.

Enzyme and pathway databases

BioCyci SSAP342451:GKFA-56-MONOMER.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
InterProi IPR006935. Helicase/UvrB_dom.
IPR014001. Helicase_ATP-bd.
IPR027417. P-loop_NTPase.
IPR007409. Restrct_endonuc_type1_HsdR_N.
IPR004473. Restrct_endonuc_typeI_HsdR.
IPR022625. TypeI_RM_Rsu_C.
[Graphical view ]
Pfami PF12008. EcoR124_C. 1 hit.
PF04313. HSDR_N. 1 hit.
PF04851. ResIII. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR00348. hsdR. 1 hit.
PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Whole genome sequence of Staphylococcus saprophyticus reveals the pathogenesis of uncomplicated urinary tract infection."
    Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.
    Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 15305 / DSM 20229.

Entry informationi

Entry nameiHSDR_STAS1
AccessioniPrimary (citable) accession number: Q4A127
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: September 13, 2005
Last modified: October 1, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Type I restriction and modification enzymes are complex, multifunctional systems which require ATP, S-adenosyl methionine and magnesium as cofactors and, in addition to their endonucleolytic and methylase activities, are potent DNA-dependent ATPases.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3