ID   HIP1_ECTSH              Reviewed;          72 AA.
AC   P38941;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=High-potential iron-sulfur protein isozyme 1;
DE            Short=HiPIP 1;
GN   Name=hip1;
OS   Ectothiorhodospira shaposhnikovii (Ectothiorhodospira vacuolata).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Ectothiorhodospira.
OX   NCBI_TaxID=1054;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   STRAIN=ATCC 43036 / DSM 2111 / Beta-1 / BN 9512;
RX   PubMed=8311477; DOI=10.1006/abbi.1994.1011;
RA   Ambler R.P., Meyer T.E., Kamen M.D.;
RT   "Amino acid sequences of two high-potential iron sulfur proteins (HiPIPs)
RT   from the moderately halophilic purple phototrophic bacterium
RT   Ectothiorhodospira vacuolata.";
RL   Arch. Biochem. Biophys. 308:78-81(1994).
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 +260 mV.;
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; S41611; S41611.
DR   AlphaFoldDB; P38941; -.
DR   SMR; P38941; -.
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; Transport.
FT   CHAIN           1..72
FT                   /note="High-potential iron-sulfur protein isozyme 1"
FT                   /id="PRO_0000220420"
FT   BINDING         34
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00705"
FT   BINDING         37
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00705"
FT   BINDING         51
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00705"
FT   BINDING         65
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00705"
SQ   SEQUENCE   72 AA;  7691 MW;  C5DD79AD593A6F54 CRC64;
     AERLDENSPE ALALNYKHDG ASVDHPSHAA GQKCINCLLY TDPSATEWGG CAVFPNKLVN
     ANGWCTAYVA RG