ID   HIP_ALLWA               Reviewed;          85 AA.
AC   B3EBZ3;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   25-JAN-2012, sequence version 1.
DT   03-AUG-2022, entry version 18.
DE   RecName: Full=High-potential iron-sulfur protein {ECO:0000303|PubMed:14562962};
DE            Short=HiPIP {ECO:0000303|PubMed:14562962};
OS   Allochromatium warmingii (Chromatium warmingii).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC   Allochromatium.
OX   NCBI_TaxID=61595;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RX   PubMed=14562962; DOI=10.1007/s00239-003-2465-y;
RA   Van Driessche G., Vandenberghe I., Devreese B., Samyn B., Meyer T.E.,
RA   Leigh R., Cusanovich M.A., Bartsch R.G., Fischer U., Van Beeumen J.J.;
RT   "Amino acid sequences and distribution of high-potential iron-sulfur
RT   proteins that donate electrons to the photosynthetic reaction center in
RT   phototropic proteobacteria.";
RL   J. Mol. Evol. 57:181-199(2003).
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. {ECO:0000250|UniProtKB:P00260,
CC       ECO:0000255|PROSITE-ProRule:PRU00705}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P59860}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P00260,
CC       ECO:0000255|PROSITE-ProRule:PRU00705}.
CC   -!- SIMILARITY: Belongs to the high-potential iron-sulfur protein (HiPIP)
CC       family. {ECO:0000255|PROSITE-ProRule:PRU00705}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   AlphaFoldDB; B3EBZ3; -.
DR   BMRB; B3EBZ3; -.
DR   SMR; B3EBZ3; -.
DR   STRING; 61595.SAMN05421644_10731; -.
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..85
FT                   /note="High-potential iron-sulfur protein"
FT                   /id="PRO_0000415399"
FT   BINDING         43
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P00260,
FT                   ECO:0000255|PROSITE-ProRule:PRU00705"
FT   BINDING         46
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P00260,
FT                   ECO:0000255|PROSITE-ProRule:PRU00705"
FT   BINDING         63
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P00260,
FT                   ECO:0000255|PROSITE-ProRule:PRU00705"
FT   BINDING         77
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000250|UniProtKB:P00260,
FT                   ECO:0000255|PROSITE-ProRule:PRU00705"
SQ   SEQUENCE   85 AA;  8937 MW;  317FF2055E8A3983 CRC64;
     SAPANAVSAD DATAIALKYN QDATKSERVS AARPGLPPEE QHCANCQFMQ ADAAGATDEW
     KGCQLFPGKL INVNGWCASW TLKAG