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Protein
Submitted name:

Uncharacterized protein

Gene
N/A
Organism
Finegoldia magna (Peptostreptococcus magnus)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi111 – 1111ZincCombined sources
Metal bindingi136 – 1361ZincCombined sources

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

Metal-bindingCombined sources, ZincCombined sources

Names & Taxonomyi

Protein namesi
Submitted name:
Uncharacterized proteinImported
OrganismiFinegoldia magna (Peptostreptococcus magnus)Imported
Taxonomic identifieri1260 [NCBI]
Taxonomic lineageiBacteriaFirmicutesTissierelliaTissierellalesPeptoniphilaceaeFinegoldia

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HZ5X-ray1.80A/B111-173[»]
1HZ6X-ray1.70A/B/C111-173[»]
1JMLX-ray1.90A111-173[»]
1K50X-ray1.80A/B/C/D111-173[»]
1K51X-ray1.80A111-173[»]
1K52X-ray1.80A/B111-173[»]
1K53X-ray2.10A/B111-173[»]
1KH0X-ray1.90A/B111-173[»]
2JZPNMR-A111-173[»]
2KACNMR-A111-173[»]
ProteinModelPortaliQ51912.
SMRiQ51912. Positions 96-173, 183-245, 248-318, 320-390, 397-463.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ51912.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini688 – 71932GRAM_POS_ANCHORINGInterPro annotationAdd
BLAST

Phylogenomic databases

eggNOGiENOG41089UU. Bacteria.
ENOG410XX92. LUCA.

Family and domain databases

InterProiIPR003147. B1_Ig_chn-bd.
IPR019948. Gram-positive_anchor.
IPR019931. LPXTG_anchor.
[Graphical view]
PfamiPF02246. B1. 5 hits.
PF00746. Gram_pos_anchor. 1 hit.
[Graphical view]
PROSITEiPS50847. GRAM_POS_ANCHORING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q51912-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALAGAIVV TGGVGSYAAD EPIDLEKLEE KRDKENVGNL PKFDNEVKDG
60 70 80 90 100
SENPMAKYPD FDDEASTRFE TENNEFEEKK VVSDNFFDQS EHPFVENKEE
110 120 130 140 150
TPETPETDSE EEVTIKANLI FANGSTQTAE FKGTFEKATS EAYAYADTLK
160 170 180 190 200
KDNGEYTVDV ADKGYTLNIK FAGKEKTPEE PKEEVTIKAN LIYADGKTQT
210 220 230 240 250
AEFKGTFEEA TAEAYRYADA LKKDNGEYTV DVADKGYTLN IKFAGKEKTP
260 270 280 290 300
EEPKEEVTIK ANLIYADGKT QTAEFKGTFE EATAEAYRYA DLLAKENGKY
310 320 330 340 350
TVDVADKGYT LNIKFAGKEK TPEEPKEEVT IKANLIYADG KTQTAEFKGT
360 370 380 390 400
FAEATAEAYR YADLLAKENG KYTADLEDGG YTINIRFAGK KVDEKPEEKE
410 420 430 440 450
QVTIKENIYF EDGTVQTATF KGTFAEATAE AYRYADLLSK EHGKYTADLE
460 470 480 490 500
DGGYTINIRF AGKEEPEETP EKPEVQDGYA SYEEAEAAAK EALKNDDVNK
510 520 530 540 550
SYTIRQGADG RYYYVLSPVE AEEEKPEAQN GYATYEEAEA AAKKALENDP
560 570 580 590 600
INKSYSIRQG ADGRYYYVLS PVEAETPEKP VEPSEPSTPD VPSNPSNPST
610 620 630 640 650
PDVPSTPDVP SNPSTPEVPS NPSTPGNEEK PGNEQKPGNE QKPGNEQKPG
660 670 680 690 700
NEQKPGNEQK PDQPSKPEKE ENGKGGVDSP KKKEKAALPK AGSEAEILTL
710
AAASLSSVAG AFISLKKRK
Length:719
Mass (Da):78,983
Last modified:November 1, 1996 - v1
Checksum:i963A8D76D5E34DD2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86697 Genomic DNA. Translation: AAA25612.1.
PIRiA42808.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86697 Genomic DNA. Translation: AAA25612.1.
PIRiA42808.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1HZ5X-ray1.80A/B111-173[»]
1HZ6X-ray1.70A/B/C111-173[»]
1JMLX-ray1.90A111-173[»]
1K50X-ray1.80A/B/C/D111-173[»]
1K51X-ray1.80A111-173[»]
1K52X-ray1.80A/B111-173[»]
1K53X-ray2.10A/B111-173[»]
1KH0X-ray1.90A/B111-173[»]
2JZPNMR-A111-173[»]
2KACNMR-A111-173[»]
ProteinModelPortaliQ51912.
SMRiQ51912. Positions 96-173, 183-245, 248-318, 320-390, 397-463.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG41089UU. Bacteria.
ENOG410XX92. LUCA.

Miscellaneous databases

EvolutionaryTraceiQ51912.

Family and domain databases

InterProiIPR003147. B1_Ig_chn-bd.
IPR019948. Gram-positive_anchor.
IPR019931. LPXTG_anchor.
[Graphical view]
PfamiPF02246. B1. 5 hits.
PF00746. Gram_pos_anchor. 1 hit.
[Graphical view]
PROSITEiPS50847. GRAM_POS_ANCHORING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Protein L, a bacterial immunoglobulin-binding protein and possible virulence determinant."
    Kastern W., Holst E., Nielsen E., Sjobring U., Bjorck L.
    Infect. Immun. 58:1217-1222(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 312Imported.
  2. "Structure of peptostreptococcal protein L and identification of a repeated immunoglobulin light chain-binding domain."
    Kastern W., Sjobring U., Bjorck L.
    J. Biol. Chem. 267:12820-12825(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 312Imported.
  3. "Structures of the B1 domain of protein L from Peptostreptococcus magnus with a tyrosine to tryptophan substitution."
    O'Neill J.W., Kim D.E., Baker D., Zhang K.Y.
    Acta Crystallogr. D 57:480-487(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 111-173 IN COMPLEX WITH ZINC.
  4. "Conversion of monomeric protein L to an obligate dimer by computational protein design."
    Kuhlman B., O'Neill J.W., Kim D.E., Zhang K.Y., Baker D.
    Proc. Natl. Acad. Sci. U.S.A. 98:10687-10691(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 111-173 IN COMPLEX WITH ZINC.
  5. "Single-site mutations induce 3D domain swapping in the B1 domain of protein L from Peptostreptococcus magnus."
    O'Neill J.W., Kim D.E., Johnsen K., Baker D., Zhang K.Y.
    Structure 9:1017-1027(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 111-173 IN COMPLEX WITH ZINC.
  6. "Accurate computer-based design of a new backbone conformation in the second turn of protein L."
    Kuhlman B., O'Neill J.W., Kim D.E., Zhang K.Y., Baker D.
    J. Mol. Biol. 315:471-477(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 111-173.
  7. "Protein stabilization and the Hofmeister effect: the role of hydrophobic solvation."
    Tadeo X., Lopez-Mendez B., Castano D., Trigueros T., Millet O.
    Biophys. J. 97:2595-2603(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 111-173.
  8. "Structural basis for the aminoacid composition of proteins from halophilic archea."
    Tadeo X., Lopez-Mendez B., Trigueros T., Lain A., Castano D., Millet O.
    PLoS Biol. 7:e1000257-e1000257(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 111-173.

Entry informationi

Entry nameiQ51912_FINMA
AccessioniPrimary (citable) accession number: Q51912
Entry historyi
Integrated into UniProtKB/TrEMBL: November 1, 1996
Last sequence update: November 1, 1996
Last modified: April 13, 2016
This is version 84 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.