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Protein
Submitted name:

Microbial serine proteinases

Gene

sub

Organism
Bacillus subtilis
Status
Unreviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi139Calcium 1Combined sources1
Metal bindingi159Calcium 1Combined sources1
Metal bindingi207Calcium 1Combined sources1
Metal bindingi323Calcium 2; via carbonyl oxygenCombined sources1
Metal bindingi326Calcium 2Combined sources1
Metal bindingi328Calcium 2; via carbonyl oxygenCombined sources1
Metal bindingi330Calcium 2Combined sources1
Metal bindingi333Calcium 2Combined sources1
Metal bindingi396Calcium 3Combined sources1
Metal bindingi397Calcium 3; via carbonyl oxygenCombined sources1
Metal bindingi404Calcium 3; via carbonyl oxygenCombined sources1
Metal bindingi406Calcium 3; via carbonyl oxygenCombined sources1
Metal bindingi408Calcium 3Combined sources1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Serine proteaseUniRule annotation

Keywords - Ligandi

CalciumCombined sources, Metal-bindingCombined sources

Enzyme and pathway databases

BRENDAi3.4.21.62. 658.

Protein family/group databases

MEROPSiS08.140.

Names & Taxonomyi

Protein namesi
Submitted name:
Microbial serine proteinasesImported (EC:3.4.21.14Imported)
Gene namesi
Name:subImported
OrganismiBacillus subtilisImported
Taxonomic identifieri1423 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Sequence analysisAdd BLAST31
ChainiPRO_500423200832 – 419Sequence analysisAdd BLAST388

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi161 ↔ 175Combined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GKOX-ray1.40A111-419[»]
ProteinModelPortaliQ45681.
SMRiQ45681.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ45681.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini135 – 406Peptidase S8InterPro annotationAdd BLAST272

Sequence similaritiesi

Belongs to the peptidase S8 family.UniRule annotation

Keywords - Domaini

SignalSequence analysis

Family and domain databases

Gene3Di3.40.50.200. 1 hit.
InterProiIPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 2 hits.
PfamiPF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q45681-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRSGKIFTT AMLAVTLMMP AIGVSANRGN AADGNEKFRV LVDSANQNNL
60 70 80 90 100
KNVKEQYGVH WDFAGEGFTT NMNEKQFNAL QNNKNLTVEK VPELEIATAT
110 120 130 140 150
NKPEALYNAM AASQSTPWGI KAIYNNSNLT STSGGAGINI AVLDTGVNTN
160 170 180 190 200
HPDLSNNVEQ CKDFTVGTNF TDNSCTDRQG HGTHVAGSAL ANGGTGSGVY
210 220 230 240 250
GVAPEADLWA YKVLGDDGSG YADDIAEAIR HAGDQATALN TKVVINMSLG
260 270 280 290 300
SSGESSLITN AVDYAYDKGV LIIAAAGNSG PKPGSIGYPG ALVNAVAVAA
310 320 330 340 350
LENTIQNGTY RVADFSSRGH KRTAGDYVIQ KGDVEISAPG AAVYSTWFDG
360 370 380 390 400
GYATISGTSM ASPHAAGLAA KIWAQSPAAS NVDVRGELQT RASVNDILSG
410
NSAGSGDDIA SGFGFAKVQ
Length:419
Mass (Da):43,346
Last modified:November 1, 1996 - v1
Checksum:i529D6F785F11CEB8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63533 Genomic DNA. Translation: CAA45096.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X63533 Genomic DNA. Translation: CAA45096.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2GKOX-ray1.40A111-419[»]
ProteinModelPortaliQ45681.
SMRiQ45681.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiS08.140.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.4.21.62. 658.

Miscellaneous databases

EvolutionaryTraceiQ45681.

Family and domain databases

Gene3Di3.40.50.200. 1 hit.
InterProiIPR000209. Peptidase_S8/S53_dom.
IPR023827. Peptidase_S8_Asp-AS.
IPR022398. Peptidase_S8_His-AS.
IPR023828. Peptidase_S8_Ser-AS.
IPR015500. Peptidase_S8_subtilisin-rel.
[Graphical view]
PANTHERiPTHR10795. PTHR10795. 2 hits.
PfamiPF00082. Peptidase_S8. 1 hit.
[Graphical view]
PRINTSiPR00723. SUBTILISIN.
SUPFAMiSSF52743. SSF52743. 1 hit.
PROSITEiPS00136. SUBTILASE_ASP. 1 hit.
PS00137. SUBTILASE_HIS. 1 hit.
PS00138. SUBTILASE_SER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiQ45681_BACIU
AccessioniPrimary (citable) accession number: Q45681
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources

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.