ID   MBHS_OLICO              Reviewed;         360 AA.
AC   O33405; Q6LB91;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   16-JUN-2009, entry version 66.
DE   RecName: Full=Uptake hydrogenase small subunit;
DE            EC=1.12.99.6;
DE   AltName: Full=Hydrogenlyase;
DE   AltName: Full=Membrane-bound hydrogenase small subunit;
DE   Flags: Precursor;
GN   Name=hoxS; OrderedLocusNames=OCAR_p_08064;
OS   Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / OM5).
OG   Plasmid megaplasmid pHCG3.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Oligotropha.
OX   NCBI_TaxID=504832;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 46-63.
RX   MEDLINE=97464431; PubMed=9324252;
RA   Santiago B., Meyer O.;
RT   "Purification and molecular characterization of the H2 uptake
RT   membrane-bound NiFe-hydrogenase from the carboxidotrophic bacterium
RT   Oligotropha carboxidovorans.";
RL   J. Bacteriol. 179:6053-6060(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14644498; DOI=10.1016/j.gene.2003.08.027;
RA   Fuhrmann S., Ferner M., Jeffke T., Henne A., Gottschalk G., Meyer O.;
RT   "Complete nucleotide sequence of the circular megaplasmid pHCG3 of
RT   Oligotropha carboxidovorans: function in the chemolithoautotrophic
RT   utilization of CO, H(2) and CO(2).";
RL   Gene 322:67-75(2003).
CC   -!- FUNCTION: This enzyme recycles the H(2) produced by nitrogenase to
CC       increase the production of ATP and to protect nitrogenase against
CC       inhibition or damage by O(2) under carbon- or phosphate-limited
CC       conditions (By similarity).
CC   -!- CATALYTIC ACTIVITY: H(2) + A = AH(2).
CC   -!- COFACTOR: Binds 2 4Fe-4S clusters.
CC   -!- COFACTOR: Binds 1 3Fe-4S cluster.
CC   -!- SUBUNIT: Heterodimer of a large and a small subunit.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of
CC       the signal peptide cleavage has been experimentally proven.
CC   -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase small
CC       subunit family.
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DR   EMBL; X82447; CAG28468.1; -; Genomic_DNA.
DR   RefSeq; YP_015635.2; -.
DR   HSSP; P18187; 1FRF.
DR   GeneID; 2807127; -.
DR   GenomeReviews; X82447_GR; OCAR_p_08064.
DR   BRENDA; 1.12.99.6; 255922.
DR   GO; GO:0009375; C:ferredoxin hydrogenase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro.
DR   GO; GO:0033748; F:hydrogenase (acceptor) activity; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro.
DR   GO; GO:0048038; F:quinone binding; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa.
DR   InterPro; IPR001821; NiFe_hydrogenase_ssu.
DR   InterPro; IPR006311; Tat.
DR   InterPro; IPR017909; Twin_arg_translocation_Tat.
DR   Pfam; PF01058; Oxidored_q6; 1.
DR   PIRSF; PIRSF000310; NiFe_hyd_ssu; 1.
DR   PRINTS; PR00614; NIHGNASESMLL.
DR   TIGRFAMs; TIGR00391; hydA; 1.
DR   TIGRFAMs; TIGR01409; TAT_signal_seq; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   3Fe-4S; 4Fe-4S; Cell membrane; Complete proteome;
KW   Direct protein sequencing; Iron; Iron-sulfur; Membrane; Metal-binding;
KW   Oxidoreductase; Plasmid; Signal.
FT   SIGNAL        1     45       Tat-type signal.
FT   CHAIN        46    360       Uptake hydrogenase small subunit.
FT                                /FTId=PRO_0000013433.
FT   METAL        62     62       Iron-sulfur 1 (4Fe-4S) (By similarity).
FT   METAL        65     65       Iron-sulfur 1 (4Fe-4S) (By similarity).
FT   METAL       160    160       Iron-sulfur 1 (4Fe-4S) (By similarity).
FT   METAL       194    194       Iron-sulfur 1 (4Fe-4S) (By similarity).
FT   METAL       232    232       Iron-sulfur 2 (4Fe-4S); via pros nitrogen
FT                                (By similarity).
FT   METAL       235    235       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       260    260       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       266    266       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       275    275       Iron-sulfur 3 (3Fe-4S) (By similarity).
FT   METAL       294    294       Iron-sulfur 3 (3Fe-4S) (By similarity).
FT   METAL       297    297       Iron-sulfur 3 (3Fe-4S) (By similarity).
FT   CONFLICT     62     62       C -> E (in Ref. 1; AA sequence).
SQ   SEQUENCE   360 AA;  39322 MW;  F4D5CB57BC1D1DA2 CRC64;
     MTPTETFYEV MRRQGVTRRS FLKFCSLTAT ALGLGPAYTS EIAHAMETKP RTPVLWLHGL
     ECTCCSESFI RSAHPLVKDV VLSMISLDYD DTLMAAAGHQ AEAALADTIE RYKGNYILAV
     EGNPPLNEDG MFCIIGGKPF VDQLRYAAKH AKAIISWGSC ASHGCVQAAR PNPTRATPVH
     QVITDKPIIK VPGCPPIAEV MTGVITYMLT FGKLPELDRT GRPKMFYSQR IHDKCYRRPH
     FDAGQFVESF DDEGARRGYC LYKVGCKGPT TYNACSTIRW NEGTSFPIQA GHGCIGCSEE
     GFWDKGSWYA RLQDIHQFGI EANADQIGGT VAVGAAGAVA AHAAVSALKR AQTKRQTTTS
//