ID   HIP_MARGR               Reviewed;          83 AA.
AC   P00262;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=High-potential iron-sulfur protein;
DE            Short=HiPIP;
GN   Name=hip;
OS   Marichromatium gracile (Chromatium gracile).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Marichromatium.
OX   NCBI_TaxID=1048;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=7451471; DOI=10.1016/s0021-9258(19)70036-2;
RA   Tedro S.M., Meyer T.E., Bartsch R.G., Kamen M.D.;
RT   "Primary structures of high potential, four-iron-sulfur ferredoxins from
RT   the purple sulfur photosynthetic bacteria, Thiocapsa roseopersicina and
RT   Chromatium gracile.";
RL   J. Biol. Chem. 256:731-735(1981).
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   -!- SUBUNIT: Homodimer. {ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the high-potential iron-sulfur protein (HiPIP)
CC       family. {ECO:0000255|PROSITE-ProRule:PRU00705}.
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DR   PIR; A00265; IHKREG.
DR   AlphaFoldDB; P00262; -.
DR   SMR; P00262; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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; -; 1.
DR   InterPro; IPR000170; High_potential_FeS_prot.
DR   InterPro; IPR036369; HIPIP_sf.
DR   Pfam; PF01355; HIPIP; 1.
DR   SUPFAM; SSF57652; SSF57652; 1.
DR   PROSITE; PS51373; HIPIP; 1.
PE   1: Evidence at protein level;
KW   4Fe-4S; Direct protein sequencing; Electron transport; Iron; Iron-sulfur;
KW   Metal-binding; Periplasm; Transport.
FT   CHAIN           1..83
FT                   /note="High-potential iron-sulfur protein"
FT                   /id="PRO_0000220415"
FT   BINDING         43
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00705"
FT   BINDING         46
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00705"
FT   BINDING         61
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00705"
FT   BINDING         75
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00705"
SQ   SEQUENCE   83 AA;  9052 MW;  BB8B13A3F9302E79 CRC64;
     EVPANAVTES DPTAVALKYH RNAEASERVA AARPGLPPEE QHCENCQFML PDQGADEWRG
     CSLFPGKLIN LDGWCASWTL RAG