HIP_MARPU
ID HIP_MARPU Reviewed; 82 AA.
AC P59860;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=High-potential iron-sulfur protein;
DE Short=HiPIP;
GN Name=hip;
OS Marichromatium purpuratum (Chromatium purpuratum).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Marichromatium.
OX NCBI_TaxID=37487;
RN [1]
RP PROTEIN SEQUENCE OF 1-25, AND CHARACTERIZATION.
RX PubMed=8672482; DOI=10.1021/bi952731v;
RA Kerfeld C.A., Chan C., Hirasawa M., Kleis-SanFrancisco S., Yeates T.O.,
RA Knaff D.B.;
RT "Isolation and characterization of soluble electron transfer proteins from
RT Chromatium purpuratum.";
RL Biochemistry 35:7812-7818(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (4FE-4S).
RX PubMed=9760225; DOI=10.1021/bi9810252;
RA Kerfeld C.A., Salmeen A.E., Yeates T.O.;
RT "Crystal structure and possible dimerization of the high-potential iron-
RT sulfur protein from Chromatium purpuratum.";
RL Biochemistry 37:13911-13917(1998).
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 PDB; 3HIP; X-ray; 2.80 A; A/B/C=1-82.
DR PDBsum; 3HIP; -.
DR AlphaFoldDB; P59860; -.
DR SMR; P59860; -.
DR EvolutionaryTrace; P59860; -.
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 3D-structure; 4Fe-4S; Direct protein sequencing; Electron transport; Iron;
KW Iron-sulfur; Metal-binding; Periplasm; Transport.
FT CHAIN 1..82
FT /note="High-potential iron-sulfur protein"
FT /id="PRO_0000220422"
FT BINDING 42
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:9760225"
FT BINDING 45
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:9760225"
FT BINDING 60
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:9760225"
FT BINDING 74
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000269|PubMed:9760225"
FT HELIX 11..16
FT /evidence="ECO:0007829|PDB:3HIP"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:3HIP"
FT HELIX 22..24
FT /evidence="ECO:0007829|PDB:3HIP"
FT HELIX 27..30
FT /evidence="ECO:0007829|PDB:3HIP"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:3HIP"
FT HELIX 37..39
FT /evidence="ECO:0007829|PDB:3HIP"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:3HIP"
FT STRAND 48..54
FT /evidence="ECO:0007829|PDB:3HIP"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:3HIP"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:3HIP"
SQ SEQUENCE 82 AA; 8753 MW; 2C875E9C8DB8E06D CRC64;
VPANAVTESD PAAVALKYHR DAASSERVAA ARPGLPPEEQ HCENCQFMNP DSAAADWKGC
QLFPGKLINL SGWCASWTLR AG