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P00800

- THER_BACTH

UniProt

P00800 - THER_BACTH

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Protein

Thermolysin

Gene

npr

Organism
Bacillus thermoproteolyticus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Extracellular zinc metalloprotease.

Catalytic activityi

Preferential cleavage: Xaa-|-Leu > Xaa-|-Phe.

Cofactori

Protein has several cofactor binding sites:
  • Ca2+Note: Binds 4 Ca(2+) ions per subunit.
  • Zn2+Note: Binds 1 zinc ion per subunit.

Temperature dependencei

Thermostable.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi289 – 2891Calcium 1
Metal bindingi291 – 2911Calcium 1
Metal bindingi293 – 2931Calcium 1; via carbonyl oxygen
Metal bindingi370 – 3701Calcium 2
Metal bindingi374 – 3741Zinc; catalytic
Active sitei375 – 37511 PublicationPROSITE-ProRule annotation
Metal bindingi378 – 3781Zinc; catalytic
Metal bindingi398 – 3981Zinc; catalytic
Metal bindingi409 – 4091Calcium 2
Metal bindingi409 – 4091Calcium 3
Metal bindingi415 – 4151Calcium 3; via carbonyl oxygen
Metal bindingi417 – 4171Calcium 2
Metal bindingi417 – 4171Calcium 3
Metal bindingi419 – 4191Calcium 2; via carbonyl oxygen
Metal bindingi422 – 4221Calcium 2
Metal bindingi422 – 4221Calcium 3
Metal bindingi425 – 4251Calcium 4; via carbonyl oxygen
Metal bindingi426 – 4261Calcium 4
Metal bindingi429 – 4291Calcium 4; via carbonyl oxygen
Metal bindingi432 – 4321Calcium 4
Active sitei463 – 4631Proton donor1 PublicationPROSITE-ProRule annotation

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW
  2. metalloendopeptidase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Protein family/group databases

MEROPSiM04.001.

Names & Taxonomyi

Protein namesi
Recommended name:
Thermolysin (EC:3.4.24.27)
Alternative name(s):
Thermostable neutral proteinase
Gene namesi
Name:npr
OrganismiBacillus thermoproteolyticus
Taxonomic identifieri1427 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828By similarityAdd
BLAST
Propeptidei29 – 232204Activation peptide2 PublicationsPRO_0000028592Add
BLAST
Chaini233 – 548316ThermolysinPRO_0000028593Add
BLAST

Keywords - PTMi

Zymogen

Interactioni

Structurei

Secondary structure

1
548
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi236 – 2438Combined sources
Beta strandi249 – 26416Combined sources
Beta strandi271 – 2755Combined sources
Beta strandi281 – 2833Combined sources
Beta strandi288 – 2947Combined sources
Helixi297 – 2993Combined sources
Helixi300 – 32021Combined sources
Turni324 – 3263Combined sources
Beta strandi332 – 34110Combined sources
Beta strandi345 – 3473Combined sources
Beta strandi349 – 3557Combined sources
Beta strandi359 – 3635Combined sources
Helixi365 – 3673Combined sources
Helixi369 – 38315Combined sources
Helixi391 – 41222Combined sources
Beta strandi418 – 4214Combined sources
Turni422 – 4243Combined sources
Beta strandi429 – 4313Combined sources
Beta strandi434 – 4385Combined sources
Helixi440 – 4434Combined sources
Helixi449 – 4513Combined sources
Helixi457 – 4615Combined sources
Turni462 – 4654Combined sources
Helixi466 – 47813Combined sources
Beta strandi480 – 4823Combined sources
Beta strandi485 – 4873Combined sources
Helixi492 – 50514Combined sources
Helixi513 – 52816Combined sources
Helixi533 – 54412Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1FJ3X-ray2.00A233-548[»]
1FJOX-ray2.00A233-548[»]
1FJQX-ray1.70A233-548[»]
1FJTX-ray2.20A233-548[»]
1FJUX-ray2.00A233-548[»]
1FJVX-ray2.00A233-548[»]
1FJWX-ray1.90A233-548[»]
1GXWX-ray2.18A233-548[»]
1HYTX-ray1.70A233-548[»]
1KEIX-ray1.60A233-548[»]
1KJOX-ray1.60A233-548[»]
1KJPX-ray1.60A233-548[»]
1KKKX-ray1.60A233-548[»]
1KL6X-ray1.80A233-548[»]
1KR6X-ray1.80A233-548[»]
1KROX-ray1.70A233-548[»]
1KS7X-ray1.70A233-548[»]
1KTOX-ray1.90A233-548[»]
1L3FX-ray2.30E233-548[»]
1LNAX-ray1.90E233-548[»]
1LNBX-ray1.80E233-548[»]
1LNCX-ray1.80E233-548[»]
1LNDX-ray1.70E233-548[»]
1LNEX-ray1.70E233-548[»]
1LNFX-ray1.70E233-548[»]
1OS0X-ray2.10A233-548[»]
1PE5X-ray1.70A233-548[»]
1PE7X-ray1.82A233-548[»]
1PE8X-ray1.80A233-548[»]
1QF0X-ray2.20A233-548[»]
1QF1X-ray2.00A233-548[»]
1QF2X-ray2.06A233-548[»]
1THLX-ray1.70A233-548[»]
1TLIX-ray2.05A233-548[»]
1TLPX-ray2.30E233-548[»]
1TLXX-ray2.10A233-548[»]
1TMNX-ray1.90E233-548[»]
1TRLNMR-A/B487-548[»]
1Y3GX-ray2.10E233-548[»]
1Z9GX-ray1.70E233-548[»]
1ZDPX-ray1.70E233-548[»]
2A7GX-ray1.85E233-548[»]
2G4ZX-ray1.98A233-548[»]
2TLIX-ray1.95A233-548[»]
2TLXX-ray1.65A233-548[»]
2TMNX-ray1.60E233-548[»]
2WHZX-ray1.75A233-548[»]
2WI0X-ray1.95A233-548[»]
3DNZX-ray1.20A233-548[»]
3DO0X-ray1.36A233-548[»]
3DO1X-ray1.33A233-548[»]
3DO2X-ray1.22A233-548[»]
3EIMX-ray1.88A233-548[»]
3F28X-ray1.68A233-548[»]
3F2PX-ray1.95A233-548[»]
3FB0X-ray1.60A233-548[»]
3FBOX-ray1.92A233-548[»]
3FCQX-ray1.75A233-548[»]
3FGDX-ray1.33A233-548[»]
3FLFX-ray1.97A233-548[»]
3FORX-ray1.93A233-548[»]
3FV4X-ray1.56A233-548[»]
3FVPX-ray1.41A233-548[»]
3FXPX-ray2.05A233-548[»]
3FXSX-ray1.55A233-548[»]
3LS7X-ray1.98A233-548[»]
3MS3X-ray1.54A233-548[»]
3MSAX-ray1.66A233-548[»]
3MSFX-ray2.09A233-548[»]
3MSNX-ray1.97A233-548[»]
3N21X-ray1.87A233-548[»]
3NN7X-ray2.05A233-548[»]
3P7PX-ray2.20E233-548[»]
3P7QX-ray2.20E233-548[»]
3P7RX-ray2.20E233-548[»]
3P7SX-ray2.20E233-548[»]
3P7TX-ray2.20E233-548[»]
3P7UX-ray2.20E233-548[»]
3P7VX-ray2.20E233-548[»]
3P7WX-ray2.20E233-548[»]
3QGOX-ray1.45A233-548[»]
3QH1X-ray1.55A233-548[»]
3QH5X-ray1.50A233-548[»]
3SSBX-ray1.80A/B233-548[»]
3T2HX-ray1.95E233-548[»]
3T2IX-ray2.10E233-548[»]
3T2JX-ray2.00E233-548[»]
3T73X-ray1.60A233-548[»]
3T74X-ray1.28A233-548[»]
3T87X-ray1.28A233-548[»]
3T8CX-ray1.66A233-548[»]
3T8DX-ray1.41A233-548[»]
3T8FX-ray1.44A233-548[»]
3T8GX-ray1.50A233-548[»]
3T8HX-ray1.45A233-548[»]
3TLIX-ray1.95A233-548[»]
3TMNX-ray1.70E233-548[»]
3ZI6X-ray2.00A233-548[»]
4D91X-ray1.90A233-548[»]
4D9WX-ray1.38A233-548[»]
4H57X-ray1.56A233-548[»]
4MTWX-ray1.32E233-548[»]
4MWPX-ray1.23E233-548[»]
4MXJX-ray1.35E233-548[»]
4MZNX-ray1.17E233-548[»]
4N4EX-ray1.13E233-548[»]
4N5PX-ray1.25E233-548[»]
4N66X-ray1.44E233-548[»]
4OI5X-ray1.30E233-548[»]
4OW3X-ray2.10A233-548[»]
4TLIX-ray1.95A233-548[»]
4TLNX-ray2.30A233-548[»]
4TMNX-ray1.70E233-548[»]
4TNLX-ray1.80A233-548[»]
5TLIX-ray2.10A233-548[»]
5TLNX-ray2.30A233-548[»]
5TMNX-ray1.60E233-548[»]
6TLIX-ray2.10A233-548[»]
6TMNX-ray1.60E233-548[»]
7TLIX-ray1.95A233-548[»]
7TLNX-ray2.30A233-548[»]
8TLIX-ray2.20A233-548[»]
8TLNX-ray1.60E233-548[»]
ProteinModelPortaliP00800.
SMRiP00800. Positions 233-548.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00800.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M4 family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.10.170.10. 1 hit.
InterProiIPR011096. FTP_domain.
IPR025711. PepSY.
IPR023612. Peptidase_M4.
IPR001570. Peptidase_M4_C_domain.
IPR013856. Peptidase_M4_domain.
[Graphical view]
PfamiPF07504. FTP. 1 hit.
PF03413. PepSY. 1 hit.
PF01447. Peptidase_M4. 1 hit.
PF02868. Peptidase_M4_C. 1 hit.
[Graphical view]
PRINTSiPR00730. THERMOLYSIN.
PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00800-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKMKMKLASF GLAAGLAAQV FLPYNALAST EHVTWNQQFQ TPQFISGDLL
60 70 80 90 100
KVNGTSPEEL VYQYVEKNEN KFKFHENAKD TLQLKEKKND NLGFTFMRFQ
110 120 130 140 150
QTYKGIPVFG AVVTSHVKDG TLTALSGTLI PNLDTKGSLK SGKKLSEKQA
160 170 180 190 200
RDIAEKDLVA NVTKEVPEYE QGKDTEFVVY VNGDEASLAY VVNLNFLTPE
210 220 230 240 250
PGNWLYIIDA VDGKILNKFN QLDAAKPGDV KSITGTSTVG VGRGVLGDQK
260 270 280 290 300
NINTTYSTYY YLQDNTRGNG IFTYDAKYRT TLPGSLWADA DNQFFASYDA
310 320 330 340 350
PAVDAHYYAG VTYDYYKNVH NRLSYDGNNA AIRSSVHYSQ GYNNAFWNGS
360 370 380 390 400
QMVYGDGDGQ TFIPLSGGID VVAHELTHAV TDYTAGLIYQ NESGAINEAI
410 420 430 440 450
SDIFGTLVEF YANKNPDWEI GEDVYTPGIS GDSLRSMSDP AKYGDPDHYS
460 470 480 490 500
KRYTGTQDNG GVHINSGIIN KAAYLISQGG THYGVSVVGI GRDKLGKIFY
510 520 530 540
RALTQYLTPT SNFSQLRAAA VQSATDLYGS TSQEVASVKQ AFDAVGVK
Length:548
Mass (Da):60,104
Last modified:April 18, 2006 - v3
Checksum:i1D6ED3A545F045C8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti269 – 2691N → D AA sequence 1 PublicationCurated
Sequence conflicti351 – 3511Q → E AA sequence 1 PublicationCurated
Sequence conflicti400 – 4001I → M in CAA54291. (PubMed:8002967)Curated
Sequence conflicti409 – 4091E → K in CAA54291. (PubMed:8002967)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76986 Genomic DNA. Translation: CAA54291.1.
PIRiI40579. HYBST.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76986 Genomic DNA. Translation: CAA54291.1 .
PIRi I40579. HYBST.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FJ3 X-ray 2.00 A 233-548 [» ]
1FJO X-ray 2.00 A 233-548 [» ]
1FJQ X-ray 1.70 A 233-548 [» ]
1FJT X-ray 2.20 A 233-548 [» ]
1FJU X-ray 2.00 A 233-548 [» ]
1FJV X-ray 2.00 A 233-548 [» ]
1FJW X-ray 1.90 A 233-548 [» ]
1GXW X-ray 2.18 A 233-548 [» ]
1HYT X-ray 1.70 A 233-548 [» ]
1KEI X-ray 1.60 A 233-548 [» ]
1KJO X-ray 1.60 A 233-548 [» ]
1KJP X-ray 1.60 A 233-548 [» ]
1KKK X-ray 1.60 A 233-548 [» ]
1KL6 X-ray 1.80 A 233-548 [» ]
1KR6 X-ray 1.80 A 233-548 [» ]
1KRO X-ray 1.70 A 233-548 [» ]
1KS7 X-ray 1.70 A 233-548 [» ]
1KTO X-ray 1.90 A 233-548 [» ]
1L3F X-ray 2.30 E 233-548 [» ]
1LNA X-ray 1.90 E 233-548 [» ]
1LNB X-ray 1.80 E 233-548 [» ]
1LNC X-ray 1.80 E 233-548 [» ]
1LND X-ray 1.70 E 233-548 [» ]
1LNE X-ray 1.70 E 233-548 [» ]
1LNF X-ray 1.70 E 233-548 [» ]
1OS0 X-ray 2.10 A 233-548 [» ]
1PE5 X-ray 1.70 A 233-548 [» ]
1PE7 X-ray 1.82 A 233-548 [» ]
1PE8 X-ray 1.80 A 233-548 [» ]
1QF0 X-ray 2.20 A 233-548 [» ]
1QF1 X-ray 2.00 A 233-548 [» ]
1QF2 X-ray 2.06 A 233-548 [» ]
1THL X-ray 1.70 A 233-548 [» ]
1TLI X-ray 2.05 A 233-548 [» ]
1TLP X-ray 2.30 E 233-548 [» ]
1TLX X-ray 2.10 A 233-548 [» ]
1TMN X-ray 1.90 E 233-548 [» ]
1TRL NMR - A/B 487-548 [» ]
1Y3G X-ray 2.10 E 233-548 [» ]
1Z9G X-ray 1.70 E 233-548 [» ]
1ZDP X-ray 1.70 E 233-548 [» ]
2A7G X-ray 1.85 E 233-548 [» ]
2G4Z X-ray 1.98 A 233-548 [» ]
2TLI X-ray 1.95 A 233-548 [» ]
2TLX X-ray 1.65 A 233-548 [» ]
2TMN X-ray 1.60 E 233-548 [» ]
2WHZ X-ray 1.75 A 233-548 [» ]
2WI0 X-ray 1.95 A 233-548 [» ]
3DNZ X-ray 1.20 A 233-548 [» ]
3DO0 X-ray 1.36 A 233-548 [» ]
3DO1 X-ray 1.33 A 233-548 [» ]
3DO2 X-ray 1.22 A 233-548 [» ]
3EIM X-ray 1.88 A 233-548 [» ]
3F28 X-ray 1.68 A 233-548 [» ]
3F2P X-ray 1.95 A 233-548 [» ]
3FB0 X-ray 1.60 A 233-548 [» ]
3FBO X-ray 1.92 A 233-548 [» ]
3FCQ X-ray 1.75 A 233-548 [» ]
3FGD X-ray 1.33 A 233-548 [» ]
3FLF X-ray 1.97 A 233-548 [» ]
3FOR X-ray 1.93 A 233-548 [» ]
3FV4 X-ray 1.56 A 233-548 [» ]
3FVP X-ray 1.41 A 233-548 [» ]
3FXP X-ray 2.05 A 233-548 [» ]
3FXS X-ray 1.55 A 233-548 [» ]
3LS7 X-ray 1.98 A 233-548 [» ]
3MS3 X-ray 1.54 A 233-548 [» ]
3MSA X-ray 1.66 A 233-548 [» ]
3MSF X-ray 2.09 A 233-548 [» ]
3MSN X-ray 1.97 A 233-548 [» ]
3N21 X-ray 1.87 A 233-548 [» ]
3NN7 X-ray 2.05 A 233-548 [» ]
3P7P X-ray 2.20 E 233-548 [» ]
3P7Q X-ray 2.20 E 233-548 [» ]
3P7R X-ray 2.20 E 233-548 [» ]
3P7S X-ray 2.20 E 233-548 [» ]
3P7T X-ray 2.20 E 233-548 [» ]
3P7U X-ray 2.20 E 233-548 [» ]
3P7V X-ray 2.20 E 233-548 [» ]
3P7W X-ray 2.20 E 233-548 [» ]
3QGO X-ray 1.45 A 233-548 [» ]
3QH1 X-ray 1.55 A 233-548 [» ]
3QH5 X-ray 1.50 A 233-548 [» ]
3SSB X-ray 1.80 A/B 233-548 [» ]
3T2H X-ray 1.95 E 233-548 [» ]
3T2I X-ray 2.10 E 233-548 [» ]
3T2J X-ray 2.00 E 233-548 [» ]
3T73 X-ray 1.60 A 233-548 [» ]
3T74 X-ray 1.28 A 233-548 [» ]
3T87 X-ray 1.28 A 233-548 [» ]
3T8C X-ray 1.66 A 233-548 [» ]
3T8D X-ray 1.41 A 233-548 [» ]
3T8F X-ray 1.44 A 233-548 [» ]
3T8G X-ray 1.50 A 233-548 [» ]
3T8H X-ray 1.45 A 233-548 [» ]
3TLI X-ray 1.95 A 233-548 [» ]
3TMN X-ray 1.70 E 233-548 [» ]
3ZI6 X-ray 2.00 A 233-548 [» ]
4D91 X-ray 1.90 A 233-548 [» ]
4D9W X-ray 1.38 A 233-548 [» ]
4H57 X-ray 1.56 A 233-548 [» ]
4MTW X-ray 1.32 E 233-548 [» ]
4MWP X-ray 1.23 E 233-548 [» ]
4MXJ X-ray 1.35 E 233-548 [» ]
4MZN X-ray 1.17 E 233-548 [» ]
4N4E X-ray 1.13 E 233-548 [» ]
4N5P X-ray 1.25 E 233-548 [» ]
4N66 X-ray 1.44 E 233-548 [» ]
4OI5 X-ray 1.30 E 233-548 [» ]
4OW3 X-ray 2.10 A 233-548 [» ]
4TLI X-ray 1.95 A 233-548 [» ]
4TLN X-ray 2.30 A 233-548 [» ]
4TMN X-ray 1.70 E 233-548 [» ]
4TNL X-ray 1.80 A 233-548 [» ]
5TLI X-ray 2.10 A 233-548 [» ]
5TLN X-ray 2.30 A 233-548 [» ]
5TMN X-ray 1.60 E 233-548 [» ]
6TLI X-ray 2.10 A 233-548 [» ]
6TMN X-ray 1.60 E 233-548 [» ]
7TLI X-ray 1.95 A 233-548 [» ]
7TLN X-ray 2.30 A 233-548 [» ]
8TLI X-ray 2.20 A 233-548 [» ]
8TLN X-ray 1.60 E 233-548 [» ]
ProteinModelPortali P00800.
SMRi P00800. Positions 233-548.
ModBasei Search...
MobiDBi Search...

Chemistry

BindingDBi P00800.
ChEMBLi CHEMBL3392.

Protein family/group databases

MEROPSi M04.001.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P00800.

Family and domain databases

Gene3Di 3.10.170.10. 1 hit.
InterProi IPR011096. FTP_domain.
IPR025711. PepSY.
IPR023612. Peptidase_M4.
IPR001570. Peptidase_M4_C_domain.
IPR013856. Peptidase_M4_domain.
[Graphical view ]
Pfami PF07504. FTP. 1 hit.
PF03413. PepSY. 1 hit.
PF01447. Peptidase_M4. 1 hit.
PF02868. Peptidase_M4_C. 1 hit.
[Graphical view ]
PRINTSi PR00730. THERMOLYSIN.
PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Cloning and expression in Bacillus subtilis of the npr gene from Bacillus thermoproteolyticus Rokko coding for the thermostable metalloprotease thermolysin."
    O'Donohue M.J., Roques B.P., Beaumont A.
    Biochem. J. 300:599-603(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: Rokko.
  2. "Amino-acid sequence of thermolysin."
    Titani K., Hermodson M.A., Ericsson L.H., Walsh K.A., Neurath H.
    Nature New Biol. 238:35-37(1972)
    Cited for: PROTEIN SEQUENCE OF 233-548.
  3. "Amino acid sequence of thermolysin. Isolation and characterization of the fragments obtained by cleavage with cyanogen bromide."
    Titani K., Hermodson M.A., Ericsson L.H., Walsh K.A., Neurath H.
    Biochemistry 11:2427-2435(1972) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 233-268; 352-400 AND 438-477.
  4. "Evidence of an essential histidine residue in thermolysin."
    Burstein Y., Walsh K.A., Neurath H.
    Biochemistry 13:205-210(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIVE SITE.
  5. "Structure of thermolysin refined at 1.6-A resolution."
    Holmes M.A., Matthews B.W.
    J. Mol. Biol. 160:623-639(1982) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
  6. "The conformation of thermolysin."
    Matthews B.W., Weaver L.H., Kester W.R.
    J. Biol. Chem. 249:8030-8044(1974) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
  7. "NMR solution structure of the C-terminal fragment 255-316 of thermolysin: a dimer formed by subunits having the native structure."
    Rico M., Jimenez M.A., Gonzalez C., de Filippis V., Fontana A.
    Biochemistry 33:14834-14847(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 487-548.
  8. "NMR solution structure of the 205-316 C-terminal fragment of thermolysin. An example of dimerization coupled to partial unfolding."
    Conejero-Lara F., Gonzalez C., Jimenez M.A., Padmanabhan S., Mateo P.L., Rico M.
    Biochemistry 36:11975-11983(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 437-548.

Entry informationi

Entry nameiTHER_BACTH
AccessioniPrimary (citable) accession number: P00800
Secondary accession number(s): Q45779
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 18, 2006
Last modified: November 26, 2014
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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

External Data

Dasty 3