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Protein

Spore coat protein A

Gene

cotA

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Involved in brown pigmentation during sporogenesis.

GO - Molecular functioni

  • copper ion binding Source: GO_Central
  • hydroquinone:oxygen oxidoreductase activity Source: CACAO
  • oxidoreductase activity, oxidizing metal ions Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Sporulation

Enzyme and pathway databases

BioCyciBSUB:BSU06300-MONOMER.
BRENDAi1.3.3.5. 658.
SABIO-RKP07788.

Names & Taxonomyi

Protein namesi
Recommended name:
Spore coat protein A
Gene namesi
Name:cotA
Synonyms:pig
Ordered Locus Names:BSU06300
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000792571 – 513Spore coat protein AAdd BLAST513

Proteomic databases

PaxDbiP07788.

Interactioni

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100003538.

Structurei

Secondary structure

1513
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi19 – 21Combined sources3
Beta strandi26 – 37Combined sources12
Beta strandi46 – 51Combined sources6
Beta strandi54 – 56Combined sources3
Beta strandi59 – 63Combined sources5
Beta strandi68 – 74Combined sources7
Helixi86 – 88Combined sources3
Beta strandi104 – 107Combined sources4
Helixi113 – 115Combined sources3
Helixi125 – 127Combined sources3
Beta strandi128 – 130Combined sources3
Beta strandi137 – 141Combined sources5
Beta strandi148 – 154Combined sources7
Turni157 – 159Combined sources3
Helixi160 – 166Combined sources7
Beta strandi169 – 175Combined sources7
Helixi177 – 182Combined sources6
Helixi187 – 189Combined sources3
Beta strandi190 – 200Combined sources11
Beta strandi210 – 214Combined sources5
Beta strandi231 – 235Combined sources5
Beta strandi238 – 240Combined sources3
Beta strandi242 – 244Combined sources3
Beta strandi247 – 256Combined sources10
Beta strandi263 – 267Combined sources5
Beta strandi273 – 278Combined sources6
Beta strandi281 – 294Combined sources14
Beta strandi299 – 305Combined sources7
Helixi307 – 309Combined sources3
Beta strandi313 – 318Combined sources6
Beta strandi322 – 325Combined sources4
Turni328 – 332Combined sources5
Beta strandi333 – 338Combined sources6
Helixi359 – 361Combined sources3
Beta strandi366 – 378Combined sources13
Beta strandi384 – 388Combined sources5
Beta strandi406 – 413Combined sources8
Beta strandi415 – 417Combined sources3
Beta strandi419 – 425Combined sources7
Beta strandi428 – 436Combined sources9
Helixi438 – 444Combined sources7
Beta strandi449 – 451Combined sources3
Helixi458 – 460Combined sources3
Beta strandi464 – 469Combined sources6
Beta strandi473 – 480Combined sources8
Beta strandi486 – 493Combined sources8
Helixi495 – 498Combined sources4
Turni499 – 501Combined sources3
Beta strandi503 – 509Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GSKX-ray1.70A1-513[»]
1OF0X-ray2.45A1-513[»]
1W6LX-ray2.00A1-513[»]
1W6WX-ray2.20A1-513[»]
1W8EX-ray2.20A1-513[»]
2BHFX-ray2.50A1-513[»]
2WSDX-ray1.60A1-513[»]
2X87X-ray2.00A1-513[»]
2X88X-ray1.80A1-513[»]
3ZDWX-ray2.45A1-513[»]
4A66X-ray1.95A1-513[»]
4A67X-ray2.10A1-513[»]
4A68X-ray2.00A1-513[»]
4AKOX-ray1.70A1-513[»]
4AKPX-ray2.00A1-513[»]
4AKQX-ray2.10A1-513[»]
4Q89X-ray2.31A/B1-513[»]
4Q8BX-ray1.91A/B1-513[»]
4YVNX-ray2.30A1-513[»]
4YVUX-ray2.30A1-513[»]
ProteinModelPortaliP07788.
SMRiP07788.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP07788.

Family & Domainsi

Sequence similaritiesi

To S.antibioticus phenoxazinone synthase (PhsA).Curated

Phylogenomic databases

eggNOGiENOG4107STQ. Bacteria.
COG2132. LUCA.
HOGENOMiHOG000096435.
InParanoidiP07788.
KOiK06324.
OMAiPYSGRYV.
PhylomeDBiP07788.

Family and domain databases

Gene3Di2.60.40.420. 3 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 2 hits.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 3 hits.

Sequencei

Sequence statusi: Complete.

P07788-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTLEKFVDAL PIPDTLKPVQ QSKEKTYYEV TMEECTHQLH RDLPPTRLWG
60 70 80 90 100
YNGLFPGPTI EVKRNENVYV KWMNNLPSTH FLPIDHTIHH SDSQHEEPEV
110 120 130 140 150
KTVVHLHGGV TPDDSDGYPE AWFSKDFEQT GPYFKREVYH YPNQQRGAIL
160 170 180 190 200
WYHDHAMALT RLNVYAGLVG AYIIHDPKEK RLKLPSDEYD VPLLITDRTI
210 220 230 240 250
NEDGSLFYPS APENPSPSLP NPSIVPAFCG ETILVNGKVW PYLEVEPRKY
260 270 280 290 300
RFRVINASNT RTYNLSLDNG GDFIQIGSDG GLLPRSVKLN SFSLAPAERY
310 320 330 340 350
DIIIDFTAYE GESIILANSA GCGGDVNPET DANIMQFRVT KPLAQKDESR
360 370 380 390 400
KPKYLASYPS VQHERIQNIR TLKLAGTQDE YGRPVLLLNN KRWHDPVTET
410 420 430 440 450
PKVGTTEIWS IINPTRGTHP IHLHLVSFRV LDRRPFDIAR YQESGELSYT
460 470 480 490 500
GPAVPPPPSE KGWKDTIQAH AGEVLRIAAT FGPYSGRYVW HCHILEHEDY
510
DMMRPMDITD PHK
Length:513
Mass (Da):58,499
Last modified:May 30, 2000 - v4
Checksum:i836B83B458D75F87
GO

Sequence cautioni

The sequence BAA22774 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAA29165 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti347 – 367DESRK…HERIQ → TKAESRSTSPHTLRYSMKDT in AAB62305 (PubMed:8969499).CuratedAdd BLAST21
Sequence conflicti414 – 420PTRGTHP → RHAEHIL in AAB62305 (PubMed:8969499).Curated7
Sequence conflicti451 – 458GPAVPPPP → VRCPAAA in AAB62305 (PubMed:8969499).Curated8

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51115 Genomic DNA. Translation: AAB62305.1.
AB007638 Genomic DNA. Translation: BAA22774.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB12449.1.
X05678 Genomic DNA. Translation: CAA29165.1. Different initiation.
X07512 Genomic DNA. Translation: CAA30392.1.
U31756 Genomic DNA. Translation: AAC44642.1.
PIRiF69604.
RefSeqiNP_388511.1. NC_000964.3.
WP_003243170.1. NZ_JNCM01000032.1.

Genome annotation databases

EnsemblBacteriaiCAB12449; CAB12449; BSU06300.
GeneIDi936023.
KEGGibsu:BSU06300.
PATRICi18972900. VBIBacSub10457_0664.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51115 Genomic DNA. Translation: AAB62305.1.
AB007638 Genomic DNA. Translation: BAA22774.1. Different initiation.
AL009126 Genomic DNA. Translation: CAB12449.1.
X05678 Genomic DNA. Translation: CAA29165.1. Different initiation.
X07512 Genomic DNA. Translation: CAA30392.1.
U31756 Genomic DNA. Translation: AAC44642.1.
PIRiF69604.
RefSeqiNP_388511.1. NC_000964.3.
WP_003243170.1. NZ_JNCM01000032.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GSKX-ray1.70A1-513[»]
1OF0X-ray2.45A1-513[»]
1W6LX-ray2.00A1-513[»]
1W6WX-ray2.20A1-513[»]
1W8EX-ray2.20A1-513[»]
2BHFX-ray2.50A1-513[»]
2WSDX-ray1.60A1-513[»]
2X87X-ray2.00A1-513[»]
2X88X-ray1.80A1-513[»]
3ZDWX-ray2.45A1-513[»]
4A66X-ray1.95A1-513[»]
4A67X-ray2.10A1-513[»]
4A68X-ray2.00A1-513[»]
4AKOX-ray1.70A1-513[»]
4AKPX-ray2.00A1-513[»]
4AKQX-ray2.10A1-513[»]
4Q89X-ray2.31A/B1-513[»]
4Q8BX-ray1.91A/B1-513[»]
4YVNX-ray2.30A1-513[»]
4YVUX-ray2.30A1-513[»]
ProteinModelPortaliP07788.
SMRiP07788.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100003538.

Proteomic databases

PaxDbiP07788.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAB12449; CAB12449; BSU06300.
GeneIDi936023.
KEGGibsu:BSU06300.
PATRICi18972900. VBIBacSub10457_0664.

Phylogenomic databases

eggNOGiENOG4107STQ. Bacteria.
COG2132. LUCA.
HOGENOMiHOG000096435.
InParanoidiP07788.
KOiK06324.
OMAiPYSGRYV.
PhylomeDBiP07788.

Enzyme and pathway databases

BioCyciBSUB:BSU06300-MONOMER.
BRENDAi1.3.3.5. 658.
SABIO-RKP07788.

Miscellaneous databases

EvolutionaryTraceiP07788.

Family and domain databases

Gene3Di2.60.40.420. 3 hits.
InterProiIPR001117. Cu-oxidase.
IPR011706. Cu-oxidase_2.
IPR011707. Cu-oxidase_3.
IPR008972. Cupredoxin.
[Graphical view]
PfamiPF00394. Cu-oxidase. 1 hit.
PF07731. Cu-oxidase_2. 1 hit.
PF07732. Cu-oxidase_3. 2 hits.
[Graphical view]
SUPFAMiSSF49503. SSF49503. 3 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiCOTA_BACSU
AccessioniPrimary (citable) accession number: P07788
Secondary accession number(s): O24818
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: May 30, 2000
Last modified: November 2, 2016
This is version 123 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

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.