ID C6S6L7_NEIML Unreviewed; 245 AA.
AC C6S6L7;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Putative peroxiredoxin/glutaredoxin family protein {ECO:0000313|EMBL:CBA05455.1};
GN OrderedLocusNames=NMO_0843 {ECO:0000313|EMBL:CBA05455.1};
OS Neisseria meningitidis (strain alpha14).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=662598 {ECO:0000313|EMBL:CBA05455.1, ECO:0000313|Proteomes:UP000002054};
RN [1] {ECO:0000313|EMBL:CBA05455.1, ECO:0000313|Proteomes:UP000002054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=alpha14 {ECO:0000313|Proteomes:UP000002054};
RX PubMed=18305155; DOI=10.1073/pnas.0800151105;
RA Schoen C., Blom J., Claus H., Schramm-Glueck A., Brandt P., Mueller T.,
RA Goesmann A., Joseph B., Konietzny S., Kurzai O., Schmitt C., Friedrich T.,
RA Linke B., Vogel U., Frosch M.;
RT "Whole-genome comparison of disease and carriage strains provides insights
RT into virulence evolution in Neisseria meningitidis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:3473-3478(2008).
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DR EMBL; AM889136; CBA05455.1; -; Genomic_DNA.
DR RefSeq; WP_015815492.1; NC_013016.1.
DR AlphaFoldDB; C6S6L7; -.
DR KEGG; nmi:NMO_0843; -.
DR HOGENOM; CLU_072440_2_2_4; -.
DR Proteomes; UP000002054; Chromosome.
DR GO; GO:0008379; F:thioredoxin peroxidase activity; IEA:InterPro.
DR GO; GO:0034599; P:cellular response to oxidative stress; IEA:InterPro.
DR CDD; cd03029; GRX_hybridPRX5; 1.
DR CDD; cd03013; PRX5_like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 2.
DR InterPro; IPR002109; Glutaredoxin.
DR InterPro; IPR011906; Glutaredoxin_dom.
DR InterPro; IPR014025; Glutaredoxin_subgr.
DR InterPro; IPR037944; PRX5-like.
DR InterPro; IPR013740; Redoxin.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR013766; Thioredoxin_domain.
DR NCBIfam; TIGR02190; GlrX-dom; 1.
DR PANTHER; PTHR10430; PEROXIREDOXIN; 1.
DR PANTHER; PTHR10430:SF16; PEROXIREDOXIN-5, MITOCHONDRIAL; 1.
DR Pfam; PF00462; Glutaredoxin; 1.
DR Pfam; PF08534; Redoxin; 1.
DR PRINTS; PR00160; GLUTAREDOXIN.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51354; GLUTAREDOXIN_2; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
FT DOMAIN 5..169
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT ACT_SITE 51
FT /note="Cysteine sulfenic acid (-SOH) intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR637944-1"
SQ SEQUENCE 245 AA; 26928 MW; BA44ADA97D3B62FD CRC64;
MALQDRTGQK VPSVVFRTRV GDTWKDVSTD DLFKGKKVVV FSLPGAFTPT CSSSHLPRYN
ELFGAFKENG VDAIYCVSVN DTFVMNAWAA EEESDNIYMI PDGNGEFTEG MGMLVGKEDL
GFGKRSWRYS MLVNDGVVEK MFIEPEELGD PFKVSDADTM LQFVAPDWKA QESVAIFTKP
GCQFCAKAKQ ALQDKGLSYE EIVLGKDATV TSVRAITGKM TAPQVFIGGK YIGGSEDLEA
YLAKN
//
