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Protein

Thermostable carboxypeptidase 1

Gene

TTHA0270

Organism
Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues, but not Pro. Has lower activity with substrates ending with Gly or Glu.1 Publication

Catalytic activityi

Release of a C-terminal amino acid with broad specificity, except for -Pro.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 1 zinc ion per subunit.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi276 – 2761Zinc; via tele nitrogen1 Publication
Active sitei277 – 2771Proton donor/acceptorBy similarity
Metal bindingi280 – 2801Zinc; via tele nitrogen1 Publication
Metal bindingi306 – 3061Zinc1 Publication

GO - Molecular functioni

  • metallocarboxypeptidase activity Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • proteolysis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Carboxypeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-284-MONOMER.

Protein family/group databases

MEROPSiM32.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Thermostable carboxypeptidase 1 (EC:3.4.17.19)
Alternative name(s):
TthCP1
Gene namesi
Ordered Locus Names:TTHA0270
OrganismiThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
Taxonomic identifieri300852 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus
Proteomesi
  • UP000000532 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 510510Thermostable carboxypeptidase 1PRO_0000428835Add
BLAST

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi300852.TTHA0270.

Structurei

Secondary structure

1
510
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 3230Combined sources
Helixi40 – 5920Combined sources
Helixi61 – 7010Combined sources
Helixi74 – 763Combined sources
Helixi82 – 9918Combined sources
Helixi102 – 12221Combined sources
Turni123 – 1264Combined sources
Helixi128 – 15023Combined sources
Helixi166 – 1727Combined sources
Helixi178 – 20023Combined sources
Helixi208 – 2125Combined sources
Helixi217 – 23115Combined sources
Helixi235 – 2373Combined sources
Beta strandi238 – 2425Combined sources
Beta strandi248 – 2525Combined sources
Beta strandi255 – 2606Combined sources
Helixi268 – 28619Combined sources
Helixi289 – 2913Combined sources
Helixi295 – 2973Combined sources
Helixi302 – 31312Combined sources
Turni314 – 3185Combined sources
Helixi320 – 33314Combined sources
Helixi335 – 3373Combined sources
Helixi342 – 3487Combined sources
Helixi358 – 3603Combined sources
Turni363 – 3653Combined sources
Helixi366 – 38116Combined sources
Helixi390 – 40213Combined sources
Beta strandi407 – 4093Combined sources
Turni410 – 4145Combined sources
Turni418 – 4225Combined sources
Helixi428 – 44821Combined sources
Helixi452 – 4565Combined sources
Helixi461 – 47010Combined sources
Helixi472 – 4743Combined sources
Helixi480 – 4889Combined sources
Helixi495 – 50814Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WGZX-ray2.60A/B/C1-510[»]
3HOAX-ray2.10A/B1-509[»]
ProteinModelPortaliQ5SLM3.
SMRiQ5SLM3. Positions 1-510.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ5SLM3.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M32 family.Curated

Phylogenomic databases

eggNOGiENOG4105CTD. Bacteria.
COG2317. LUCA.
HOGENOMiHOG000040803.
KOiK01299.
OMAiEFGHALY.
OrthoDBiEOG64XXH7.
PhylomeDBiQ5SLM3.

Family and domain databases

InterProiIPR001333. Peptidase_M32.
[Graphical view]
PfamiPF02074. Peptidase_M32. 1 hit.
[Graphical view]
PIRSFiPIRSF006615. Zn_crbxpep_Taq. 1 hit.
PRINTSiPR00998. CRBOXYPTASET.

Sequencei

Sequence statusi: Complete.

Q5SLM3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTPEAAYQNL LEFQRETAYL ASLGALAAWD QRTMIPKKGH EHRARQMAAL
60 70 80 90 100
ARLLHQRMTD PRIGEWLEKV EGSPLVQDPL SDAAVNVREW RQAYERARAI
110 120 130 140 150
PERLAVELAQ AESEAESFWE EARPRDDWRG FLPYLKRVYA LTKEKAEVLF
160 170 180 190 200
ALPPAPGDPP YGELYDALLD GYEPGMRARE LLPLFAELKE GLKGLLDRIL
210 220 230 240 250
GSGKRPDTSI LHRPYPVEAQ RRFALELLSA CGYDLEAGRL DPTAHPFEIA
260 270 280 290 300
IGPGDVRITT RYYEDFFNAG IFGTLHEMGH ALYEQGLPKE HWGTPRGDAV
310 320 330 340 350
SLGVHESQSR TWENLVGRSL GFWERFFPRA REVFASLGDV SLEDFHFAVN
360 370 380 390 400
AVEPSLIRVE ADEVTYNLHI LVRLELELAL FRGELSPEDL PEAWAEKYRD
410 420 430 440 450
HLGVAPKDYK DGVMQDVHWA GGLFGYFPTY TLGNLYAAQF FQKAEAELGP
460 470 480 490 500
LEPRFARGEF QPFLDWTRAR IHAEGSRFRP RVLVERVTGE APSARPFLAY
510
LEKKYAALYG
Length:510
Mass (Da):58,014
Last modified:December 21, 2004 - v1
Checksum:i6EE48D42AA2FA379
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70093.1.
RefSeqiWP_011174078.1. NC_006461.1.
YP_143536.1. NC_006461.1.

Genome annotation databases

EnsemblBacteriaiBAD70093; BAD70093; BAD70093.
GeneIDi3168368.
KEGGittj:TTHA0270.
PATRICi23955495. VBITheThe93045_0270.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP008226 Genomic DNA. Translation: BAD70093.1.
RefSeqiWP_011174078.1. NC_006461.1.
YP_143536.1. NC_006461.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WGZX-ray2.60A/B/C1-510[»]
3HOAX-ray2.10A/B1-509[»]
ProteinModelPortaliQ5SLM3.
SMRiQ5SLM3. Positions 1-510.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi300852.TTHA0270.

Protein family/group databases

MEROPSiM32.001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAD70093; BAD70093; BAD70093.
GeneIDi3168368.
KEGGittj:TTHA0270.
PATRICi23955495. VBITheThe93045_0270.

Phylogenomic databases

eggNOGiENOG4105CTD. Bacteria.
COG2317. LUCA.
HOGENOMiHOG000040803.
KOiK01299.
OMAiEFGHALY.
OrthoDBiEOG64XXH7.
PhylomeDBiQ5SLM3.

Enzyme and pathway databases

BioCyciTTHE300852:GH8R-284-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ5SLM3.

Family and domain databases

InterProiIPR001333. Peptidase_M32.
[Graphical view]
PfamiPF02074. Peptidase_M32. 1 hit.
[Graphical view]
PIRSFiPIRSF006615. Zn_crbxpep_Taq. 1 hit.
PRINTSiPR00998. CRBOXYPTASET.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Complete genome sequence of Thermus thermophilus HB8."
    Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HB8 / ATCC 27634 / DSM 579.
  2. "Crystallization and preliminary X-ray analysis of carboxypeptidase 1 from Thermus thermophilus."
    Nagata K., Tsutsui S., Lee W.C., Ito K., Kamo M., Inoue Y., Tanokura M.
    Acta Crystallogr. D 60:1445-1446(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) IN COMPLEX WITH ZINC.
    Strain: HB8 / ATCC 27634 / DSM 579.
  3. "Insight into the substrate length restriction of M32 carboxypeptidases: characterization of two distinct subfamilies."
    Lee M.M., Isaza C.E., White J.D., Chen R.P., Liang G.F., He H.T., Chan S.I., Chan M.K.
    Proteins 77:647-657(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH ZINC IONS, COFACTOR, CATALYTIC ACTIVITY, SUBUNIT, FUNCTION.
    Strain: HB8 / ATCC 27634 / DSM 579.

Entry informationi

Entry nameiCBP1_THET8
AccessioniPrimary (citable) accession number: Q5SLM3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: December 21, 2004
Last modified: January 20, 2016
This is version 63 of the entry and version 1 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

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.