HYPC_ECOLI
ID HYPC_ECOLI Reviewed; 90 AA.
AC P0AAM3; P24191; Q2MAA1;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Hydrogenase maturation factor HypC {ECO:0000305};
DE AltName: Full=Chaperone-type protein HypC {ECO:0000303|PubMed:10783387};
DE AltName: Full=Hydrogenase accessory chaperone HypC {ECO:0000305};
GN Name=hypC {ECO:0000303|PubMed:1849603}; OrderedLocusNames=b2728, JW2698;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1849603; DOI=10.1111/j.1365-2958.1991.tb01833.x;
RA Lutz S., Jacobi A., Schlensog V., Boehm R., Sawers G., Boeck A.;
RT "Molecular characterization of an operon (hyp) necessary for the activity
RT of the three hydrogenase isoenzymes in Escherichia coli.";
RL Mol. Microbiol. 5:123-135(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [5]
RP SUBUNIT, AND INTERACTION WITH HYCE.
RX PubMed=9485446; DOI=10.1021/bi9720078;
RA Drapal N., Boeck A.;
RT "Interaction of the hydrogenase accessory protein HypC with HycE, the large
RT subunit of Escherichia coli hydrogenase 3 during enzyme maturation.";
RL Biochemistry 37:2941-2948(1998).
RN [6]
RP FUNCTION, INTERACTION WITH HYCE, AND MUTAGENESIS OF CYS-2 AND PRO-6.
RX PubMed=10783387; DOI=10.1074/jbc.m000987200;
RA Magalon A., Bock A.;
RT "Analysis of the HypC-hycE complex, a key intermediate in the assembly of
RT the metal center of the Escherichia coli hydrogenase 3.";
RL J. Biol. Chem. 275:21114-21120(2000).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11292801; DOI=10.1128/jb.183.9.2817-2822.2001;
RA Blokesch M., Magalon A., Boeck A.;
RT "Interplay between the specific chaperone-like proteins HybG and HypC in
RT maturation of hydrogenases 1, 2, and 3 from Escherichia coli.";
RL J. Bacteriol. 183:2817-2822(2001).
RN [8]
RP INTERACTION WITH HYCE AND HYPD, AND MUTAGENESIS OF CYS-2 AND PRO-6.
RX PubMed=12441107; DOI=10.1016/s0022-2836(02)01070-7;
RA Blokesch M., Boeck A.;
RT "Maturation of [NiFe]-hydrogenases in Escherichia coli: the HypC cycle.";
RL J. Mol. Biol. 324:287-296(2002).
RN [9]
RP FUNCTION, AND INTERACTION WITH HYPD AND HYPE.
RX PubMed=15504408; DOI=10.1016/j.jmb.2004.09.040;
RA Blokesch M., Albracht S.P., Matzanke B.F., Drapal N.M., Jacobi A.,
RA Boeck A.;
RT "The complex between hydrogenase-maturation proteins HypC and HypD is an
RT intermediate in the supply of cyanide to the active site iron of [NiFe]-
RT hydrogenases.";
RL J. Mol. Biol. 344:155-167(2004).
RN [10]
RP FUNCTION, AND INTERACTION WITH HYPD.
RX PubMed=23022438; DOI=10.1016/j.febslet.2012.09.019;
RA Soboh B., Stripp S.T., Muhr E., Granich C., Braussemann M., Herzberg M.,
RA Heberle J., Gary Sawers R.;
RT "[NiFe]-hydrogenase maturation: isolation of a HypC-HypD complex carrying
RT diatomic CO and CN- ligands.";
RL FEBS Lett. 586:3882-3887(2012).
RN [11]
RP FUNCTION, AND MUTAGENESIS OF CYS-2 AND HIS-51.
RX PubMed=23851071; DOI=10.1016/j.febslet.2013.06.055;
RA Soboh B., Stripp S.T., Bielak C., Lindenstrauss U., Braussemann M.,
RA Javaid M., Hallensleben M., Granich C., Herzberg M., Heberle J.,
RA Sawers R.G.;
RT "The [NiFe]-hydrogenase accessory chaperones HypC and HybG of Escherichia
RT coli are iron- and carbon dioxide-binding proteins.";
RL FEBS Lett. 587:2512-2516(2013).
RN [12] {ECO:0007744|PDB:2OT2}
RP STRUCTURE BY NMR.
RX PubMed=17669368; DOI=10.1016/j.bbrc.2007.07.094;
RA Wang L., Xia B., Jin C.;
RT "Solution structure of Escherichia coli HypC.";
RL Biochem. Biophys. Res. Commun. 361:665-669(2007).
CC -!- FUNCTION: Involved in the maturation of [NiFe] hydrogenases. Involved
CC in the biosynthesis of the Fe(CN)(2)CO cofactor (PubMed:15504408,
CC PubMed:23022438). HypC delivers iron-bound CO(2) to HypD where
CC reduction to CO probably occurs (PubMed:23851071). In complex with
CC HypD, accepts the cyanide ligand generated by HypF and HypE, and also
CC coordinates the carbon monoxide ligand (PubMed:15504408,
CC PubMed:23022438). Involved in the maturation of the hydrogenase 3
CC (PubMed:10783387, PubMed:11292801). Also participates in the maturation
CC of hydrogenase 1 (PubMed:11292801). {ECO:0000269|PubMed:10783387,
CC ECO:0000269|PubMed:11292801, ECO:0000269|PubMed:15504408,
CC ECO:0000269|PubMed:23022438, ECO:0000269|PubMed:23851071}.
CC -!- PATHWAY: Protein modification; [NiFe] hydrogenase maturation.
CC {ECO:0000305}.
CC -!- SUBUNIT: Homodimer (PubMed:9485446). Interacts with HypD
CC (PubMed:12441107, PubMed:15504408, PubMed:23022438). Also forms a
CC complex with HypD and HypE (PubMed:15504408). Interacts with the
CC precursor form of HycE (pre-HycE), the large subunit of hydrogenase 3
CC (PubMed:9485446, PubMed:10783387, PubMed:12441107).
CC {ECO:0000269|PubMed:10783387, ECO:0000269|PubMed:12441107,
CC ECO:0000269|PubMed:15504408, ECO:0000269|PubMed:23022438,
CC ECO:0000269|PubMed:9485446}.
CC -!- INTERACTION:
CC P0AAM3; P0A8N3: lysS; NbExp=3; IntAct=EBI-552654, EBI-552719;
CC -!- DISRUPTION PHENOTYPE: Deletion of both hybG and hypC completely
CC abolishes hydrogenase activity. {ECO:0000269|PubMed:11292801}.
CC -!- SIMILARITY: Belongs to the HupF/HypC family. {ECO:0000305}.
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DR EMBL; X54543; CAA38414.1; -; Genomic_DNA.
DR EMBL; U29579; AAA69238.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75770.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76805.1; -; Genomic_DNA.
DR PIR; S15199; S15199.
DR RefSeq; NP_417208.1; NC_000913.3.
DR RefSeq; WP_000334881.1; NZ_STEB01000027.1.
DR PDB; 2OT2; NMR; -; A=1-90.
DR PDBsum; 2OT2; -.
DR AlphaFoldDB; P0AAM3; -.
DR BMRB; P0AAM3; -.
DR SMR; P0AAM3; -.
DR BioGRID; 4261426; 9.
DR BioGRID; 851524; 1.
DR ComplexPortal; CPX-5284; HypCDE Ni-hydrogenase maturation complex.
DR DIP; DIP-36430N; -.
DR IntAct; P0AAM3; 9.
DR STRING; 511145.b2728; -.
DR PaxDb; P0AAM3; -.
DR EnsemblBacteria; AAC75770; AAC75770; b2728.
DR EnsemblBacteria; BAE76805; BAE76805; BAE76805.
DR GeneID; 67413974; -.
DR GeneID; 947192; -.
DR KEGG; ecj:JW2698; -.
DR KEGG; eco:b2728; -.
DR PATRIC; fig|1411691.4.peg.4013; -.
DR EchoBASE; EB0480; -.
DR eggNOG; COG0298; Bacteria.
DR HOGENOM; CLU_159381_1_1_6; -.
DR InParanoid; P0AAM3; -.
DR OMA; MCLAIPC; -.
DR PhylomeDB; P0AAM3; -.
DR BioCyc; EcoCyc:EG10485-MON; -.
DR BioCyc; MetaCyc:EG10485-MON; -.
DR UniPathway; UPA00335; -.
DR EvolutionaryTrace; P0AAM3; -.
DR PRO; PR:P0AAM3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:1902670; F:carbon dioxide binding; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0005506; F:iron ion binding; IDA:EcoCyc.
DR GO; GO:0051604; P:protein maturation; IDA:EcoCyc.
DR InterPro; IPR019812; Hydgase_assmbl_chp_CS.
DR InterPro; IPR001109; Hydrogenase_HupF/HypC.
DR PANTHER; PTHR35177; PTHR35177; 1.
DR Pfam; PF01455; HupF_HypC; 1.
DR PRINTS; PR00445; HUPFHYPC.
DR TIGRFAMs; TIGR00074; hypC_hupF; 1.
DR PROSITE; PS01097; HUPF_HYPC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305|PubMed:10783387"
FT CHAIN 2..90
FT /note="Hydrogenase maturation factor HypC"
FT /id="PRO_0000201398"
FT SITE 2
FT /note="Important for interaction with HypD and the
FT precursor form of hydrogenase"
FT /evidence="ECO:0000269|PubMed:10783387,
FT ECO:0000269|PubMed:12441107"
FT MUTAGEN 2
FT /note="C->A: Lack of hydrogenase 3 activity. Cannot
FT interact with pre-HycE or HypD. Does not bind iron."
FT /evidence="ECO:0000269|PubMed:10783387,
FT ECO:0000269|PubMed:12441107, ECO:0000269|PubMed:23851071"
FT MUTAGEN 2
FT /note="C->R,S: Lack of hydrogenase 3 activity. Cannot
FT interact with pre-HycE or HypD."
FT /evidence="ECO:0000269|PubMed:10783387,
FT ECO:0000269|PubMed:12441107"
FT MUTAGEN 6
FT /note="P->A,T: No change in hydrogenase 3 activity. Does
FT not affect interaction with HypD."
FT /evidence="ECO:0000269|PubMed:10783387,
FT ECO:0000269|PubMed:12441107"
FT MUTAGEN 51
FT /note="H->R: Does not bind iron."
FT /evidence="ECO:0000269|PubMed:23851071"
FT STRAND 4..12
FT /evidence="ECO:0007829|PDB:2OT2"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:2OT2"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:2OT2"
FT TURN 31..33
FT /evidence="ECO:0007829|PDB:2OT2"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:2OT2"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:2OT2"
FT HELIX 61..76
FT /evidence="ECO:0007829|PDB:2OT2"
FT HELIX 80..85
FT /evidence="ECO:0007829|PDB:2OT2"
SQ SEQUENCE 90 AA; 9732 MW; FBE252F1875C7879 CRC64;
MCIGVPGQIR TIDGNQAKVD VCGIQRDVDL TLVGSCDENG QPRVGQWVLV HVGFAMSVIN
EAEARDTLDA LQNMFDVEPD VGALLYGEEK
