ID   HIP_THETI               Reviewed;          83 AA.
AC   P80176;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-MAY-2023, entry version 98.
DE   RecName: Full=High-potential iron-sulfur protein;
DE            Short=HiPIP;
GN   Name=hip;
OS   Thermochromatium tepidum (Chromatium tepidum).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Thermochromatium.
OX   NCBI_TaxID=1050;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 43061 / DSM 3771 / MC;
RX   PubMed=8393645; DOI=10.1006/abbi.1993.1409;
RA   Moulis J.-M., Scherrer N., Gagnon J., Forest E., Petillot Y., Garcia D.;
RT   "Primary structure of Chromatium tepidum high-potential iron-sulfur protein
RT   in relation to thermal denaturation.";
RL   Arch. Biochem. Biophys. 305:186-192(1993).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (4FE-4S).
RX   PubMed=11095707; DOI=10.1073/pnas.240224997;
RA   Nogi T., Fathir I., Kobayashi M., Nozawa T., Miki K.;
RT   "Crystal structures of photosynthetic reaction center and high-potential
RT   iron-sulfur protein from Thermochromatium tepidum: thermostability and
RT   electron transfer.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:13561-13566(2000).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (0.8 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (4FE-4S).
RX   PubMed=12077426; DOI=10.1107/s0907444902006261;
RA   Liu L., Nogi T., Kobayashi M., Nozawa T., Miki K.;
RT   "Ultrahigh-resolution structure of high-potential iron-sulfur protein from
RT   Thermochromatium tepidum.";
RL   Acta Crystallogr. D 58:1085-1091(2002).
CC   -!- FUNCTION: Specific class of high-redox-potential 4Fe-4S ferredoxins.
CC       Functions in anaerobic electron transport in most purple and in some
CC       other photosynthetic bacteria and in at least one genus (Paracoccus) of
CC       halophilic, denitrifying bacteria.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Redox potential:
CC         E(0) is +323 mV.;
CC       Temperature dependence:
CC         Thermostable.;
CC   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the high-potential iron-sulfur protein (HiPIP)
CC       family. {ECO:0000255|PROSITE-ProRule:PRU00705}.
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DR   PIR; S35586; S35586.
DR   PDB; 1EYT; X-ray; 1.50 A; A=1-83.
DR   PDB; 1IUA; X-ray; 0.80 A; A=1-83.
DR   PDB; 2AMS; X-ray; 1.40 A; A=1-83.
DR   PDB; 2FLA; X-ray; 0.95 A; A=1-83.
DR   PDB; 3A38; X-ray; 0.70 A; A=1-83.
DR   PDB; 3A39; X-ray; 0.72 A; A=1-83.
DR   PDB; 5D8V; X-ray; 0.48 A; A=1-83.
DR   PDB; 5WQQ; X-ray; 0.80 A; A=1-83.
DR   PDB; 5WQR; X-ray; 0.80 A; A=1-83.
DR   PDB; 6AIQ; X-ray; 0.85 A; A=1-83.
DR   PDB; 6AIR; X-ray; 0.85 A; A=1-83.
DR   PDB; 7C52; X-ray; 2.89 A; b=1-83.
DR   PDB; 7VOS; Other; 0.66 A; A=1-83.
DR   PDBsum; 1EYT; -.
DR   PDBsum; 1IUA; -.
DR   PDBsum; 2AMS; -.
DR   PDBsum; 2FLA; -.
DR   PDBsum; 3A38; -.
DR   PDBsum; 3A39; -.
DR   PDBsum; 5D8V; -.
DR   PDBsum; 5WQQ; -.
DR   PDBsum; 5WQR; -.
DR   PDBsum; 6AIQ; -.
DR   PDBsum; 6AIR; -.
DR   PDBsum; 7C52; -.
DR   PDBsum; 7VOS; -.
DR   AlphaFoldDB; P80176; -.
DR   SMR; P80176; -.
DR   EvolutionaryTrace; P80176; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019646; P:aerobic electron transport chain; IEA:InterPro.
DR   Gene3D; 4.10.490.10; High potential iron-sulphur protein; 1.
DR   InterPro; IPR000170; High_potential_FeS_prot.
DR   InterPro; IPR036369; HIPIP_sf.
DR   Pfam; PF01355; HIPIP; 1.
DR   SUPFAM; SSF57652; HIPIP (high potential iron protein); 1.
DR   PROSITE; PS51373; HIPIP; 1.
PE   1: Evidence at protein level;
KW   3D-structure; 4Fe-4S; Direct protein sequencing; Electron transport; Iron;
KW   Iron-sulfur; Metal-binding; Transport.
FT   CHAIN           1..83
FT                   /note="High-potential iron-sulfur protein"
FT                   /id="PRO_0000220429"
FT   BINDING         43
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:11095707,
FT                   ECO:0000269|PubMed:12077426"
FT   BINDING         46
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:11095707,
FT                   ECO:0000269|PubMed:12077426"
FT   BINDING         61
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:11095707,
FT                   ECO:0000269|PubMed:12077426"
FT   BINDING         75
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:11095707,
FT                   ECO:0000269|PubMed:12077426"
FT   HELIX           12..17
FT                   /evidence="ECO:0007829|PDB:5D8V"
FT   STRAND          20..22
FT                   /evidence="ECO:0007829|PDB:5D8V"
FT   HELIX           23..25
FT                   /evidence="ECO:0007829|PDB:5D8V"
FT   HELIX           28..31
FT                   /evidence="ECO:0007829|PDB:5D8V"
FT   HELIX           38..40
FT                   /evidence="ECO:0007829|PDB:5D8V"
FT   HELIX           43..45
FT                   /evidence="ECO:0007829|PDB:5D8V"
FT   STRAND          49..55
FT                   /evidence="ECO:0007829|PDB:5D8V"
FT   STRAND          58..61
FT                   /evidence="ECO:0007829|PDB:5D8V"
FT   STRAND          68..70
FT                   /evidence="ECO:0007829|PDB:5D8V"
SQ   SEQUENCE   83 AA;  8786 MW;  92116E4FD2C44E0A CRC64;
     AAPANAVTAD DPTAIALKYN QDATKSERVA AARPGLPPEE QHCANCQFMQ ANVGEGDWKG
     CQLFPGKLIN VNGWCASWTL KAG
//