Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P00800

- THER_BACTH

UniProt

P00800 - THER_BACTH

Protein

Thermolysin

Gene

npr

Organism
Bacillus thermoproteolyticus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 3 (18 Apr 2006)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Extracellular zinc metalloprotease.

    Catalytic activityi

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

    Cofactori

    Binds 4 calcium ions per subunit.
    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

    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-SubCell

    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 – 2438
    Beta strandi249 – 26416
    Beta strandi271 – 2755
    Beta strandi281 – 2833
    Beta strandi288 – 2947
    Helixi297 – 2993
    Helixi300 – 32021
    Turni324 – 3263
    Beta strandi332 – 34110
    Beta strandi345 – 3473
    Beta strandi349 – 3557
    Beta strandi359 – 3635
    Helixi365 – 3673
    Helixi369 – 38315
    Helixi391 – 41222
    Beta strandi418 – 4214
    Turni422 – 4243
    Beta strandi429 – 4313
    Beta strandi434 – 4385
    Helixi440 – 4434
    Helixi449 – 4513
    Helixi457 – 4615
    Turni462 – 4654
    Helixi466 – 47813
    Beta strandi480 – 4823
    Beta strandi485 – 4873
    Helixi492 – 50514
    Helixi513 – 52816
    Helixi533 – 54412

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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

    MKMKMKLASF GLAAGLAAQV FLPYNALAST EHVTWNQQFQ TPQFISGDLL    50
    KVNGTSPEEL VYQYVEKNEN KFKFHENAKD TLQLKEKKND NLGFTFMRFQ 100
    QTYKGIPVFG AVVTSHVKDG TLTALSGTLI PNLDTKGSLK SGKKLSEKQA 150
    RDIAEKDLVA NVTKEVPEYE QGKDTEFVVY VNGDEASLAY VVNLNFLTPE 200
    PGNWLYIIDA VDGKILNKFN QLDAAKPGDV KSITGTSTVG VGRGVLGDQK 250
    NINTTYSTYY YLQDNTRGNG IFTYDAKYRT TLPGSLWADA DNQFFASYDA 300
    PAVDAHYYAG VTYDYYKNVH NRLSYDGNNA AIRSSVHYSQ GYNNAFWNGS 350
    QMVYGDGDGQ TFIPLSGGID VVAHELTHAV TDYTAGLIYQ NESGAINEAI 400
    SDIFGTLVEF YANKNPDWEI GEDVYTPGIS GDSLRSMSDP AKYGDPDHYS 450
    KRYTGTQDNG GVHINSGIIN KAAYLISQGG THYGVSVVGI GRDKLGKIFY 500
    RALTQYLTPT SNFSQLRAAA VQSATDLYGS TSQEVASVKQ AFDAVGVK 548
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76986 Genomic DNA. Translation: CAA54291.1.
    PIRiI40579. HYBST.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X76986 Genomic DNA. Translation: CAA54291.1 .
    PIRi I40579. HYBST.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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 [» ]
    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: October 1, 2014
    This is version 127 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