ID   MBHS_WOLSU              Reviewed;         354 AA.
AC   P31884;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 2.
DT   25-NOV-2008, entry version 69.
DE   RecName: Full=Quinone-reactive Ni/Fe-hydrogenase small chain;
DE            EC=1.12.5.1;
DE   AltName: Full=Membrane-bound hydrogenase small subunit;
DE   AltName: Full=Hydrogen:quinone oxidoreductase;
DE   Flags: Precursor;
GN   Name=hydA; OrderedLocusNames=WS1687;
OS   Wolinella succinogenes.
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Wolinella.
OX   NCBI_TaxID=844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 37-52.
RX   MEDLINE=92267032; PubMed=1587288;
RA   Dross F., Geisler V., Lenger R., Theis F., Krafft T., Fahrenholz F.,
RA   Kojro E., Duchene A., Tripier D., Juvenal K., Kroeger A.;
RT   "The quinone-reactive Ni/Fe-hydrogenase of Wolinella succinogenes.";
RL   Eur. J. Biochem. 206:93-102(1992).
RN   [2]
RP   ERRATUM.
RX   MEDLINE=93307313; PubMed=8319698;
RA   Dross F., Geisler V., Lenger R., Theis F., Krafft T., Fahrenholz F.,
RA   Kojro E., Duchene A., Tripier D., Juvenal K., Kroeger A.;
RL   Eur. J. Biochem. 214:949-950(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSMZ 1740;
RX   MEDLINE=22882897; PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA   Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA   Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA   Meyer F., Lederer H., Schuster S.C.;
RT   "Complete genome sequence and analysis of Wolinella succinogenes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
CC   -!- CATALYTIC ACTIVITY: H(2) + menaquinone = menaquinol.
CC   -!- COFACTOR: Binds 1 3Fe-4S cluster (By similarity).
CC   -!- COFACTOR: Binds 2 4Fe-4S clusters (By similarity).
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; X65189; CAA46302.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BX571661; CAE10714.1; ALT_INIT; Genomic_DNA.
DR   PIR; S33852; S33852.
DR   RefSeq; NP_907814.1; -.
DR   HSSP; P18187; 1FRF.
DR   GeneID; 2554748; -.
DR   GenomeReviews; BX571656_GR; WS1687.
DR   KEGG; wsu:WS1687; -.
DR   NMPDR; fig|273121.1.peg.1541; -.
DR   HOGENOM; P31884; -.
DR   BioCyc; WSUC273121:WS1687-MON; -.
DR   GO; GO:0009375; C:ferredoxin hydrogenase complex; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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:0047067; F:hydrogen:quinone oxidoreductase 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:0006120; P:mitochondrial electron transport, NADH to u...; IEA:InterPro.
DR   InterPro; IPR001821; NiFe_hyd_ssu.
DR   InterPro; IPR013634; NiFe_hyd_ssu_N.
DR   InterPro; IPR006137; OxRdtase_q6.
DR   InterPro; IPR006311; Tat.
DR   Pfam; PF08425; NiFe_dehyd_N; 1.
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; Signal.
FT   SIGNAL        1     36       Tat-type signal.
FT   CHAIN        37    354       Quinone-reactive Ni/Fe-hydrogenase small
FT                                chain.
FT                                /FTId=PRO_0000013437.
FT   METAL        53     53       Iron-sulfur 1 (4Fe-4S) (By similarity).
FT   METAL        56     56       Iron-sulfur 1 (4Fe-4S) (By similarity).
FT   METAL       153    153       Iron-sulfur 1 (4Fe-4S) (By similarity).
FT   METAL       186    186       Iron-sulfur 1 (4Fe-4S) (By similarity).
FT   METAL       224    224       Iron-sulfur 2 (4Fe-4S); via pros nitrogen
FT                                (By similarity).
FT   METAL       227    227       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       252    252       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       258    258       Iron-sulfur 2 (4Fe-4S) (By similarity).
FT   METAL       267    267       Iron-sulfur 3 (3Fe-4S) (By similarity).
FT   METAL       286    286       Iron-sulfur 3 (3Fe-4S) (By similarity).
FT   METAL       289    289       Iron-sulfur 3 (3Fe-4S) (By similarity).
SQ   SEQUENCE   354 AA;  38294 MW;  C39CC21D2F5AB7D0 CRC64;
     MLEEKGIERR DFMKWAGAMT AMLSLPATFT PLTAKAAELA DRLPVIWLHM AECTGCSESL
     LRTDGPGIDS LIFDYISLEY HETVMAAAGW QAEHNLEHAI EKYKGRYVLM VEGGIPAGSS
     EFYLTVGPHG TTGAEHARHA SANAAAIFAI GSCSSFGGVQ AARPNPTNAQ PLSKVTNKPV
     INVPGCPPSE KNIVGNVLHF ILFGTLPSVD AFNRPMWAYG LRIHDLCERR GRFDAGEFVQ
     EFGDEGAKKG YCLYKVGCKG PYTFNNCSKL RFNQHTSWPV QAGHGCIGCS EPDFWDTMGP
     FEEPVANRLY ATAFDGLGAD KTADKIGITL LAATAVGVAA HAVLSMMVKD KENN
//