Outer membrane protein p64k or PM-6 - Neisseria meningitidis

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Unreviewed, UniProtKB/TrEMBL Q51225 (Q51225_NEIME)

Last modified June 16, 2009. Version 62. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequences · References · Cross-references · Entry information

Names and origin

Protein names

Submitted name:
Outer membrane protein p64k or PM-6 EMBL CAA54878.1

Gene names

Name:

m-6 EMBL CAA54878.1

Organism

Neisseria meningitidis EMBL CAA54878.1

Taxonomic identifier

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	594 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Sequence similarities

Contains 1 lipoyl-binding domain. RuleBase RU000447V1

Ontologies

Keywords
Domain	Lipoyl RuleBase RU000447V1
Gene Ontology (GO)
Biological process	cell redox homeostasis Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro dihydrolipoyl dehydrogenase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

Sequence

Length

Mass (Da)

Tools

Q51225-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 24823E854A29CA62
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594

61,883

        10         20         30         40         50         60 
MALVELKVPD IGGHENVDII AVEVNVGDTI AVDDTLITLE TDKATMDVPA EVAGVVKEVK 

        70         80         90        100        110        120 
VKVGDKISEG GLIVVVEAEG TAAAPKAEAA AAPAQEAPKA AAPAPQAAQF GGSADAEYDV 

       130        140        150        160        170        180 
VVLGGGPGGY SAAFAAADEG LKVAIVERYK TLGGVCLNVG CIPSKALLHN AAVIDEVRHL 

       190        200        210        220        230        240 
AANGIKYPEP ELDIDMLRAY KDGVVSRLTG GLAGMAKSRK VDVIQGDGQF LDPHHLEVSL 

       250        260        270        280        290        300 
TAGDAYEQAA PTGEKKIVAF KNCIIAAGSR VTKLPFIPED PRIIDSSGAL ALKEVPGKLL 

       310        320        330        340        350        360 
IIGGGIIGLE MGTVYSTLGS RLDVVEMMDG LMQGADRDLV KVWQKQNEYR FDNIMVNTKT 

       370        380        390        400        410        420 
VAVEPKEDGV YVTFEGANAP KEPQRYDAVL VAAGRAPNGK LISAEKAGVA VTDRGFIEVD 

       430        440        450        460        470        480 
KQMRTNVPHI YAIGDIVGQP MLAHKAVHEG HVAAENCAGH KAYFDARVIP GVAYTSPEVA 

       490        500        510        520        530        540 
WVGETELSAK ASGRKITKAN FPWAASGRAI ANGCDKPFTK LIFDAETGRI IGGGIVGPNG 

       550        560        570        580        590 
GDMIGEVCLA IEMGCDAADI GKTIHPHPTL GESIGMAAEV ALGTCTDLPP QKKK

References

[1]	"Characterisation of the lpdA gene from Neisseria meningitidis by polymerase chain reaction, restriction fragment length polymorphism and sequencing." Silva R., Menendez T., Alonso L.M., Iglesias E., Musacchio A., de Jesus Leal M., Alvarez A., Couizeau E., Martin A., Herrera L.S., Guillen G. FEMS Microbiol. Lett. 174:191-199(1999) [PubMed: 10234839] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: B:4:P1.15 EMBL CAA54878.1.
[2]	Guillen G.G.G.N. Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: B:4:P1.15 EMBL CAA54878.1.
[3]	"Molecular structure of the lipoamide dehydrogenase domain of a surface antigen from Neisseria meningitidis." Li de la Sierra I., Pernot L., Prange T., Saludjian P., Schiltz M., Fourme R., Padron G. J. Mol. Biol. 269:129-141(1997) [PubMed: 9193005] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 112-593.

Cross-references

Sequence databases

X77920 Genomic DNA. Translation: CAA54878.1.

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1BHY	X-ray	4.18	A	112-593	[»]
1OJT	X-ray	2.75	A	112-593	[»]

ModBase

Family and domain databases

InterPro

IPR003016. 2-oxoA_DH_lipoyl-BS.
IPR000089. Biotin_lipoyl.
IPR013027. FAD_pyr_nucl-diS_OxRdtase.
IPR000815. Hg_reductase.
IPR006258. Lipoamide_DH.
IPR004099. Pyr_nucl-diS_OxRdtase_dimer.
IPR012999. Pyr_OxRdtase_I_AS.
IPR001327. Pyr_OxRdtase_NAD_bd.
[Graphical view]

Gene3D

G3DSA:3.30.390.30. Pyr_redox_dim. 1 hit.

PANTHER

PTHR22912:SF20. Lipoamide_DH. 1 hit.

Pfam

PF00364. Biotin_lipoyl. 1 hit.
PF00070. Pyr_redox. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
PF02852. Pyr_redox_dim. 1 hit.
[Graphical view]

PRINTS

PR00368. FADPNR.
PR00945. HGRDTASE.

ProDom

PD000139. FAD_pyr_redox. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01350. lipoamide_DH. 1 hit.

PROSITE

PS50968. BIOTINYL_LIPOYL. 1 hit.
PS00189. LIPOYL. 1 hit.
PS00076. PYRIDINE_REDOX_1. 1 hit.
[Graphical view]

ProtoNet

Other Resources

LinkHub

Entry information

Entry name

Q51225_NEIME

Accession

Primary (citable) accession number: Q51225

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	November 1, 1996
Last modified:	June 16, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequences · References · Cross-references · Entry information