ID   PHFS_CUPO1              Reviewed;         124 AA.
AC   P13628;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Periplasmic [Fe] hydrogenase small subunit;
DE            EC=1.12.7.2;
DE   AltName: Full=Fe hydrogenlyase small chain;
DE   Flags: Precursor;
GN   Name=hydB;
OS   Cupidesulfovibrio oxamicus (strain Monticello) (Desulfovibrio vulgaris
OS   subsp. oxamicus).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Cupidesulfovibrio.
OX   NCBI_TaxID=884;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2661538; DOI=10.1128/jb.171.7.3881-3889.1989;
RA   Voordouw G., Strang J.D., Wilson F.R.;
RT   "Organization of the genes encoding [Fe] hydrogenase in Desulfovibrio
RT   vulgaris subsp. oxamicus Monticello.";
RL   J. Bacteriol. 171:3881-3889(1989).
CC   -!- FUNCTION: May be involved in hydrogen uptake for the reduction of
CC       sulfate to hydrogen sulfide in an electron transport chain. Cytochrome
CC       c3 is likely to be the physiological electron carrier for the enzyme.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2 + 2 oxidized [2Fe-2S]-[ferredoxin] = 2 H(+) + 2 reduced
CC         [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:17445, Rhea:RHEA-COMP:10000,
CC         Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15378, ChEBI:CHEBI:18276,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738; EC=1.12.7.2;
CC   -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has not been experimentally proven.
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DR   EMBL; M27212; AAA23374.1; -; Genomic_DNA.
DR   PIR; B32886; HQDVSV.
DR   AlphaFoldDB; P13628; -.
DR   SMR; P13628; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.260.20; -; 1.
DR   InterPro; IPR008953; Fe_hydrogenase_HydB.
DR   InterPro; IPR003149; Fe_hydrogenase_ssu.
DR   InterPro; IPR036991; Fe_hydrogenase_ssu_sf.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   Pfam; PF02256; Fe_hyd_SSU; 1.
DR   SMART; SM00902; Fe_hyd_SSU; 1.
DR   SUPFAM; SSF48674; SSF48674; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Iron; Iron-sulfur; Metal-binding; Oxidoreductase; Periplasm; Signal.
FT   SIGNAL          1..34
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648"
FT   CHAIN           35..124
FT                   /note="Periplasmic [Fe] hydrogenase small subunit"
FT                   /id="PRO_0000013414"
FT   REGION          103..124
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   124 AA;  13962 MW;  296AF34FD32B21B5 CRC64;
     MQIVNLTRRG FLKAACVVTG GALISIRMTG KAVAAAKQLK DYMMDRINGV YGADAKFPVR
     ASQDNVQVQK LYADFLEKPM SHKAEQLLHT HWVDRSKAIE RMKAQGAYPN PRAKEFEGNT
     YPYE