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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=MS11A;
PubMed=2854063 [NCBI, ExPASy, EBI, Israel, Japan]
Taha M.K.,
So M.,
Seifert H.S.,
Billyard E.,
Marchal C.;
"Pilin expression in Neisseria gonorrhoeae is under both positive and negative transcriptional control.";
EMBO J. 7:4367-4378(1988).
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[2]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Lowther W.T.,
Brot N.,
Weissbach H.,
Honek J.F.,
Matthews B.W.;
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
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[3]
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IDENTIFICATION OF PEPTIDE METHIONINE SULFOXIDE REDUCTASE ACTIVITY.
DOI=10.1073/pnas.93.15.7985; PubMed=8755589 [NCBI, ExPASy, EBI, Israel, Japan]
Wizemann T.M.,
Moskovitz J.,
Pearce B.J.,
Cundell D.,
Arvidson C.G.,
So M.,
Weissbach H.,
Brot N.,
Masure H.R.;
"Peptide methionine sulfoxide reductase contributes to the maintenance of adhesins in three major pathogens.";
Proc. Natl. Acad. Sci. U.S.A. 93:7985-7990(1996).
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- FUNCTION: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation (By similarity). Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. PilB mutants have been shown to be hyperpiliated and hyperadherent.
- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (S)-S-oxide + thioredoxin.
- CATALYTIC ACTIVITY: L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S-oxide + thioredoxin.
- CATALYTIC ACTIVITY: Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L-methionine (R)-S-oxide + thioredoxin.
- DOMAIN: Possesses 2 methionine sulfoxide reductase domains (A/MsrA and B/MsrB) and 1 N-terminal thioredoxin domain. The domain B exhibits a thioredoxin dependent methionine sulfoxide reductase activity; the Cys-495 is probably involved in the reduction of MetSO and in formation of the sulfenic acid derivative. The regeneration of Cys-495 is probably done via formation of a disulfide bond with Cys-440 followed by its reduction by thioredoxin.
- SIMILARITY: In the N-terminal section; belongs to the thioredoxin family.
- SIMILARITY: In the central section; belongs to the msrA Met sulfoxide reductase family.
- SIMILARITY: In the C-terminal section; belongs to the msrB Met sulfoxide reductase family.
- SIMILARITY: Contains 1 thioredoxin domain.
- CAUTION: Was originally (Ref.1) thought to play a role along with pilA in the transcription regulation of pilE.
- SEQUENCE CAUTION:
- Sequence=CAA32146.1; Type=Frameshift; Positions=Several;
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 522 AA [This is the length of the unprocessed precursor] |
Molecular weight: 57959 Da [This is the MW of the unprocessed precursor] |
CRC64: DDC8EC308B57B30C [This is a checksum on the sequence] |
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10 20 30 40 50 60
MKHRTFFSLC AKFGCLLALG ACSPKIVDAG TATVPHTLST LKTADNRPAS VYLKKDKPTL
70 80 90 100 110 120
IKFWASWCPL CLSELGQAEK WAQDAKFSSA NLITVASPGF LHEKKDGEFQ KWYAGLNYPK
130 140 150 160 170 180
LPVVTDNGGT IAQNLNISVY PSWALIGKDG DVQRIVKGSI NEAQALALIR NPNADLGSLK
190 200 210 220 230 240
HSFYKPDTQK KDSAIMNTRT IYLAGGCFWG LEAYFQRIDG VVDAVSGYAN GNTENPSYED
250 260 270 280 290 300
VSYRHTGHAE TVKVTYDADK LSLDDILQYY FRVVDPTSLN KQGNDTGTQY RSGVYYTDPA
310 320 330 340 350 360
EKAVIAAALK REQQKYQLPL VVENEPLKNF YDAEEYHQDY LIKNPNGYCH IDIRKADEPL
370 380 390 400 410 420
PGKTKAAPQG KGFDAATYKK PSDAELKRTL TEEQYQVTQN SATEYAFSHE YDHLFKPGIY
430 440 450 460 470 480
VDVVSGEPLF SSADKYDSGC GWPSFTRPID AKSVTEHDDF SFNMRRTEVR SRAADSHLGH
490 500 510 520
VFPDGPRDKG GLRYCINGAS LKFIPLEQMD AAGYGALKGE VK
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P14930 in FASTA format |
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