1N68,2UXT,1PF3


Conserved Protein Domain Family
CuRO_3_CueO_FtsP

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cd13890: CuRO_3_CueO_FtsP 
Click on image for an interactive view with Cn3D
The third Cupredoxin domain of the multicopper oxidase CueO, the cell division protein FtsP, and similar proteins
CueO is a multicopper oxidase (MCO) that is part of the copper-regulatory cue operon, which employs a cytosolic metalloregulatory protein CueR that induces expression of CopA and CueO under copper stress conditions. CueO is a periplasmic multicopper oxidase that is stimulated by exogenous copper(II). FtsP (also named SufI) is a component of the cell division apparatus. It is involved in protecting or stabilizing the assembly of divisomes under stress conditions. FtsP belongs to the multicopper oxidase superfamily but lacks metal cofactors. The protein is localized at septal rings and may serve as a scaffolding function. Members of this subfamily contain three cupredoxin domains and this model represents the first domain. Although MCOs have diverse functions, majority of them have three cupredoxin domain repeats that include one mononuclear and one trinuclear copper center. The copper ions are bound in several sites: Type 1, Type 2, and/or Type 3. The ensemble of types 2 and 3 copper is called a trinuclear cluster. MCOs oxidize their substrate by accepting electrons at a mononuclear copper center and transferring them to the active site trinuclear copper center. The cupredoxin domain 3 of 3-domain MCOs contains the Type 1 (T1) copper binding site and part the trinuclear copper binding site, which is located at the interface of domains 1 and 3. FtsP does not contain any copper binding sites.
Statistics
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PSSM-Id: 259957
Aligned: 41 rows
Threshold Bit Score: 154.329
Created: 7-Nov-2012
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 4 residues -Click on image for an interactive view with Cn3D
Feature 1: Type 1 (T1) Cu binding site [ion binding site], 4 residue positions
Conserved feature residue pattern:H C H XClick to see conserved feature residue pattern help
Evidence:
  • Comment:Type 1 (T1) copper sites are characterized by their conserved H...C...H...M copper ligands.
  • Comment:Some members bind copper at the T1 site with three amino acid residues (HCH), instead of four (HCHM).

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                                     
1N68_A    317 GLTVRKLQLSMdpmldmmgmqmlmekygdqamagmdh--------sqmmghmghgnmnhmnhggkfdfhhaNKINGQAFD 388 Escherichia coli
2UXT_A    323 PIRSRDISLGDd-----------------------------------------------------------PGINGQLWD 343 Escherichia coli
1PF3_A    317 GLTVRKLQLSMdpmldmmgmqmlmekygdqamagmdh--------sqmmghmghgnmnhmnhggkfdfhhaNKINGQAFD 388
CAJ12700  454 SVQRRSFFFDErmaenmklmmrqpssnphasgddmdhmemgsmagmdhdmhgsrsaadagpaldaltsgvqMAIADKPFD 533 Brucella melitensi...
Q4QMG3    351 VAQTREFNIDVt----------------------------------------------------------nGLINQRRFD 372 Haemophilus influe...
B8F891    348 ITQERKINLRPq----------------------------------------------------------dRLINHQRFD 369 Haemophilus parasu...
B4F2J0    352 SIQPRTIQLQNs----------------------------------------------------------pPGINNARWE 373 Proteus mirabilis ...
A6VR21    348 ILQERAFHFDAe----------------------------------------------------------nAMINNKRFD 369 Actinobacillus suc...
Q9CPE1    351 VVQERQFHFDVn----------------------------------------------------------tGMVNDKHFD 372 Pasteurella multoc...
B0UVZ0    349 NMKTREFYFDVs----------------------------------------------------------nATINQQRFE 370 Haemophilus somnus...
Feature 1                               #                                                     
1N68_A    389 MnkPMFAAAKgQYERWVISGvgdmMLHPFHIHGTQFRILSengkppaaHRAGWKDTVKVEg-NVSEVLVKFNHdapkeHA 467 Escherichia coli
2UXT_A    344 VnrIDVTAQQgTWERWTVRAd---EPQAFHIEGVMFQIRNvngampfpEDRGWKDTVWVD--GQVELLVYFGQpswahFP 418 Escherichia coli
1PF3_A    389 MnkPMFAAAKgQYERWVISGvgdmLLHPFHIHGTQFRILSengkppaaHRAGWKDTVKVEg-NVSEVLVKFNHdapkeHA 467
CAJ12700  534 MerIDVEAKLgSWEIWELTSr--eMAHPFHIHGASFRILSmngkkppaHQTGWKDTALID--GKAEILVHFDReaarsHP 609 Brucella melitensi...
Q4QMG3    373 PrkVDVMARKgTIERWILNAs---LPVGFTIQGAKFVVESqgehqlqaEELAWKDTVWVK--NKTQILVKFDQassgnFP 447 Haemophilus influe...
B8F891    370 PkrIDFTVKKgTVERWYLTTt---EEVGFTLQGAKFMVETrnrqavphKQLAWRDCVWLEptQETTLLVKFEHtaseqQP 446 Haemophilus parasu...
B4F2J0    374 LsrIDLVGKQnGWERWLVTVe---TPQPFHIEGARFKVINhdgqkpapADFGWKDTVWIE--KQSELLVELKQpsyshFP 448 Proteus mirabilis ...
A6VR21    370 PrrIDVNAKQgSAERWTLSAt---NAMGFRIQGAKFVVESrddvatpgNELVWQDTLWFE--RTAKILVKFEHsasnsQP 444 Actinobacillus suc...
Q9CPE1    373 Pk-RVTNAKLnTTERWTLTAn---GIMGFRIQGAKFLIESindtsveqSEIAWKDSVLIN--GKVQILVKFEHmssnnHP 446 Pasteurella multoc...
B0UVZ0    371 PnrIDISTKRgQIERWILSSs---RPVGFKIQGARFVMKSindqpveqSDIAWKDSLWID--GKVEILVQFNHasstkFP 445 Haemophilus somnus...
Feature 1         #    #    #      
1N68_A    468 YMAHCHLLEHEDTGMMLGFTV 488 Escherichia coli
2UXT_A    419 FYFNSQTLEMADRGSIGQLLV 439 Escherichia coli
1PF3_A    468 YMAHCHLLEHEDTGMMLGFTV 488
CAJ12700  610 FMFHCHLLEHEDVGMMAQFVT 630 Brucella melitensis biovar Abortus 2308
Q4QMG3    448 FLFGVSNLMLEDMGCLGVLMV 468 Haemophilus influenzae 6P18H1
B8F891    447 FTFGVSDLMLRDRGCMGQFVV 467 Haemophilus parasuis SH0165
B4F2J0    449 FVYYSQILENADKGIAGQMEI 469 Proteus mirabilis WGLW4
A6VR21    445 FTFGSSDLMQADKGALGLIVV 465 Actinobacillus succinogenes 130Z
Q9CPE1    447 FLFGSANLMLADKGCIRLLVV 467 Pasteurella multocida subsp. multocida str. Pm70
B0UVZ0    446 FIFGSSDLVLADQGCLGSIVV 466 Haemophilus somnus 2336

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