ID   DNRN_NEIGO              Reviewed;         157 AA.
AC   D6JLP0;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Iron-sulfur cluster repair protein DnrN;
GN   Name=dnrN; ORFNames=NGNG_00128;
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33084 / F62 / M-1914;
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Young S.K., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T., Shenoy N.,
RA   Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C., Rice P.,
RA   Seifert H., Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Neisseria gonorrhoeae strain F62.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION IN REPAIR OF IRON-SULFUR CENTERS, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 33084 / F62 / M-1914;
RX   PubMed=18203837; DOI=10.1128/jb.01733-07;
RA   Overton T.W., Justino M.C., Li Y., Baptista J.M., Melo A.M., Cole J.A.,
RA   Saraiva L.M.;
RT   "Widespread distribution in pathogenic bacteria of di-iron proteins that
RT   repair oxidative and nitrosative damage to iron-sulfur centers.";
RL   J. Bacteriol. 190:2004-2013(2008).
CC   -!- FUNCTION: Di-iron-containing protein involved in the repair of iron-
CC       sulfur clusters damaged by oxidative and nitrosative stress conditions.
CC       Required to repair damage caused by nitric oxide to FNR and NsrR
CC       transcription factors. {ECO:0000269|PubMed:18203837}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- DISRUPTION PHENOTYPE: Mutant is more sensitive to damage induced by a
CC       sudden exposure to nitric oxide and is more sensitive to hydrogen
CC       peroxide. {ECO:0000269|PubMed:18203837}.
CC   -!- SIMILARITY: Belongs to the RIC family. {ECO:0000305}.
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DR   EMBL; GG749389; EFF39466.2; -; Genomic_DNA.
DR   RefSeq; WP_003688853.1; NZ_WHPL01000002.1.
DR   AlphaFoldDB; D6JLP0; -.
DR   SMR; D6JLP0; -.
DR   PRIDE; D6JLP0; -.
DR   GeneID; 66752992; -.
DR   OMA; ACTTWRV; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030091; P:protein repair; IMP:UniProtKB.
DR   GO; GO:0051409; P:response to nitrosative stress; IMP:UniProtKB.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR   InterPro; IPR012312; Hemerythrin-like.
DR   InterPro; IPR019903; RIC_family.
DR   PANTHER; PTHR36438; PTHR36438; 1.
DR   Pfam; PF01814; Hemerythrin; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Iron; Metal-binding; Stress response.
FT   CHAIN           1..157
FT                   /note="Iron-sulfur cluster repair protein DnrN"
FT                   /id="PRO_0000406194"
SQ   SEQUENCE   157 AA;  17814 MW;  94AD46E15E4F18F8 CRC64;
     MTDFSVWEAA PFGATVDHIL QRYHNVHRAQ FEELVPLAQK VAQVHADTFP AEIAGLLADM
     RDELLMHMMK EERMLFPMIN QGVGRGAAMP ISVMMHEHEE HDRAIARLKE LTGNFHAPEG
     ACGSWTRLYA LAKEMADDLN DHIHLENDIL FARVLDS