ID   HIP2_ECTSH              Reviewed;          71 AA.
AC   P38524;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=High-potential iron-sulfur protein isozyme 2;
DE            Short=HiPIP 2;
GN   Name=hip2;
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).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (4FE-4S).
RC   STRAIN=ATCC 43036 / DSM 2111 / Beta-1 / BN 9512;
RX   PubMed=8117708; DOI=10.1021/bi00175a016;
RA   Benning M.M., Meyer T.E., Rayment I., Holden H.M.;
RT   "Molecular structure of the oxidized high-potential iron-sulfur protein
RT   isolated from Ectothiorhodospira vacuolata.";
RL   Biochemistry 33:2476-2483(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 +150 mV.;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the high-potential iron-sulfur protein (HiPIP)
CC       family. {ECO:0000255|PROSITE-ProRule:PRU00705}.
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DR   PIR; S41614; S41614.
DR   PDB; 1HPI; X-ray; 1.80 A; A=1-71.
DR   PDBsum; 1HPI; -.
DR   AlphaFoldDB; P38524; -.
DR   SMR; P38524; -.
DR   EvolutionaryTrace; P38524; -.
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   3D-structure; 4Fe-4S; Direct protein sequencing; Electron transport; Iron;
KW   Iron-sulfur; Metal-binding; Transport.
FT   CHAIN           1..71
FT                   /note="High-potential iron-sulfur protein isozyme 2"
FT                   /id="PRO_0000220421"
FT   BINDING         34
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:8117708"
FT   BINDING         37
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:8117708"
FT   BINDING         51
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:8117708"
FT   BINDING         65
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000269|PubMed:8117708"
FT   HELIX           9..13
FT                   /evidence="ECO:0007829|PDB:1HPI"
FT   HELIX           20..22
FT                   /evidence="ECO:0007829|PDB:1HPI"
FT   HELIX           34..36
FT                   /evidence="ECO:0007829|PDB:1HPI"
FT   STRAND          46..51
FT                   /evidence="ECO:0007829|PDB:1HPI"
FT   STRAND          57..60
FT                   /evidence="ECO:0007829|PDB:1HPI"
SQ   SEQUENCE   71 AA;  7819 MW;  EE2FA335594898C7 CRC64;
     MERLSEDDPA AQALEYRHDA SSVQHPAYEE GQTCLNCLLY TDASAQDWGP CSVFPGKLVS
     ANGWCTAWVA R