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- SASDDA3: ATP-dependent Clp protease ATP-binding subunit ClpC1, second state -

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Basic information

Entry
Database: SASBDB / ID: SASDDA3
SampleATP-dependent Clp protease ATP-binding subunit ClpC1, second state
  • ATP-dependent Clp protease ATP-binding subunit ClpC1 (protein), ClpC1, Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function / homology
Function and homology information


protein folding chaperone / peptidoglycan-based cell wall / protein homodimerization activity / ATP hydrolysis activity / ATP binding / plasma membrane / cytosol
Similarity search - Function
UVR domain / UVR domain profile. / ClpA/B, conserved site 1 / Chaperonins clpA/B signature 1. / ClpA/ClpB, AAA lid domain / AAA lid domain / Clp repeat (R) N-terminal domain / : / Clp, repeat (R) domain / Clp repeat (R) domain profile. ...UVR domain / UVR domain profile. / ClpA/B, conserved site 1 / Chaperonins clpA/B signature 1. / ClpA/ClpB, AAA lid domain / AAA lid domain / Clp repeat (R) N-terminal domain / : / Clp, repeat (R) domain / Clp repeat (R) domain profile. / Clp, N-terminal domain superfamily / ClpA/B family / Clp ATPase, C-terminal / C-terminal, D2-small domain, of ClpB protein / C-terminal, D2-small domain, of ClpB protein / AAA domain (Cdc48 subfamily) / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
ATP-dependent Clp protease ATP-binding subunit ClpC1
Similarity search - Component
Biological speciesMycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (bacteria)
CitationDate: 2018 Jun 1
Title: The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 fromMycobacterium tuberculosis
Authors: Weinhäupl K / Brennich M / Kazmaier U / Lelievre J / Ballell L / Goldberg A / Schanda P
Contact author
  • Martha Brennich (EMBL, European Molecular Biology Laboratory (EMBL) - Grenoble Outstation, Grenoble, France)

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Structure visualization

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Models

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Sample

SampleName: ATP-dependent Clp protease ATP-binding subunit ClpC1, second state
BufferName: Hepes 50 mM pH 7.5, KCl 100 mM, glycerol 10%, MgCl2 4 mM and ATP 1 mM
pH: 7.5
Entity #957Name: ClpC1 / Type: protein
Description: ATP-dependent Clp protease ATP-binding subunit ClpC1
Formula weight: 94.518
Source: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
References: UniProt: P9WPC9
Sequence: MFERFTDRAR RVVVLAQEEA RMLNHNYIGT EHILLGLIHE GEGVAAKSLE SLGISLEGVR SQVEEIIGQG QQAPSGHIPF TPRAKKVLEL SLREALQLGH NYIGTEHILL GLIREGEGVA AQVLVKLGAE LTRVRQQVIQ LLSGYQGKEA AEAGTGGRGG ESGSPSTSLV ...Sequence:
MFERFTDRAR RVVVLAQEEA RMLNHNYIGT EHILLGLIHE GEGVAAKSLE SLGISLEGVR SQVEEIIGQG QQAPSGHIPF TPRAKKVLEL SLREALQLGH NYIGTEHILL GLIREGEGVA AQVLVKLGAE LTRVRQQVIQ LLSGYQGKEA AEAGTGGRGG ESGSPSTSLV LDQFGRNLTA AAMEGKLDPV IGREKEIERV MQVLSRRTKN NPVLIGEPGV GKTAVVEGLA QAIVHGEVPE TLKDKQLYTL DLGSLVAGSR YRGDFEERLK KVLKEINTRG DIILFIDELH TLVGAGAAEG AIDAASILKP KLARGELQTI GATTLDEYRK YIEKDAALER RFQPVQVGEP TVEHTIEILK GLRDRYEAHH RVSITDAAMV AAATLADRYI NDRFLPDKAI DLIDEAGARM RIRRMTAPPD LREFDEKIAE ARREKESAID AQDFEKAASL RDREKTLVAQ RAEREKQWRS GDLDVVAEVD DEQIAEVLGN WTGIPVFKLT EAETTRLLRM EEELHKRIIG QEDAVKAVSK AIRRTRAGLK DPKRPSGSFI FAGPSGVGKT ELSKALANFL FGDDDALIQI DMGEFHDRFT ASRLFGAPPG YVGYEEGGQL TEKVRRKPFS VVLFDEIEKA HQEIYNSLLQ VLEDGRLTDG QGRTVDFKNT VLIFTSNLGT SDISKPVGLG FSKGGGENDY ERMKQKVNDE LKKHFRPEFL NRIDDIIVFH QLTREEIIRM VDLMISRVAG QLKSKDMALV LTDAAKALLA KRGFDPVLGA RPLRRTIQRE IEDQLSEKIL FEEVGPGQVV TVDVDNWDGE GPGEDAVFTF TGTRKPPAEP DLAKAGAHSA GGPEPAARGS HHHHHH

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Experimental information

BeamInstrument name: ESRF BM29 / City: Grenoble / 国: France / Type of source: X-ray synchrotron / Wavelength: 0.099 Å / Dist. spec. to detc.: 2.867 mm
DetectorName: Pilatus 1M
Scan
Title: ATP-dependent Clp protease ATP-binding subunit ClpC1, second state
Measurement date: Sep 18, 2017 / Storage temperature: 20 °C / Cell temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 50 / Unit: 1/nm /
MinMax
Q0.0949 1.4431
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 196 /
MinMax
Q0.0948738 1.01093
P(R) point1 196
R0 25.1
Result
Type of curve: other /
ExperimentalPorod
MW1400 kDa1400 kDa
Volume-2416 nm3

P(R)P(R) errorGuinierGuinier error
Forward scattering, I0152 0.1 151.16 0.37
Radius of gyration, Rg7.984 nm0.07 7.89 nm0.07

MinMax
D-25.1
Guinier point1 15

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