IMCH_GEOSL
ID IMCH_GEOSL Reviewed; 507 AA.
AC Q747K6;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Cytochrome c-type protein ImcH {ECO:0000303|PubMed:25425235};
DE AltName: Full=Inner membrane cytochrome H {ECO:0000303|PubMed:25425235};
DE AltName: Full=Multiheme c-type cytochrome {ECO:0000303|PubMed:25425235};
GN Name=imcH {ECO:0000303|PubMed:25425235};
GN OrderedLocusNames=GSU3259 {ECO:0000312|EMBL:AAR36650.1};
OS Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Geobacteraceae; Geobacter.
OX NCBI_TaxID=243231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX PubMed=14671304; DOI=10.1126/science.1088727;
RA Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA Lovley D.R., Fraser C.M.;
RT "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT environments.";
RL Science 302:1967-1969(2003).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX PubMed=25425235; DOI=10.1128/mbio.02034-14;
RA Levar C.E., Chan C.H., Mehta-Kolte M.G., Bond D.R.;
RT "An inner membrane cytochrome required only for reduction of high redox
RT potential extracellular electron acceptors.";
RL MBio 5:E02034-E02034(2014).
CC -!- FUNCTION: Redox protein involved in a high-potential metal respiratory
CC pathway. Is required only for electron transfer to terminal
CC extracellular electron acceptors with redox potentials higher than -0.1
CC V. ImcH likely transfers electrons from the quinone pool to a
CC periplasmic acceptor. {ECO:0000269|PubMed:25425235}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:25425235}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:25425235}.
CC -!- PTM: Binds 4 heme c groups covalently per subunit.
CC {ECO:0000305|PubMed:25425235}.
CC -!- DISRUPTION PHENOTYPE: Disruption of this gene eliminates the ability of
CC G.sulfurreducens to reduce soluble Fe(III) citrate, Fe(III)-EDTA, and
CC insoluble Mn(IV) oxides, electron acceptors with potentials greater
CC than 0.1 V versus the standard hydrogen electrode (SHE), but the imcH
CC mutant retains the ability to reduce Fe(III) oxides with potentials of
CC <-0.1 V versus SHE. The imcH mutant fails to grow on electrodes poised
CC at +0.24 V versus SHE, but switching electrodes to -0.1 V versus SHE
CC triggers exponential growth. Growth with fumarate as the electron
CC acceptor is unaffected in the deletion mutant.
CC {ECO:0000269|PubMed:25425235}.
CC -!- SIMILARITY: Belongs to the NapC/NirT/NrfH family. {ECO:0000305}.
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DR EMBL; AE017180; AAR36650.1; -; Genomic_DNA.
DR RefSeq; NP_954300.1; NC_002939.5.
DR RefSeq; WP_010943871.1; NC_002939.5.
DR AlphaFoldDB; Q747K6; -.
DR STRING; 243231.GSU3259; -.
DR EnsemblBacteria; AAR36650; AAR36650; GSU3259.
DR KEGG; gsu:GSU3259; -.
DR PATRIC; fig|243231.5.peg.3276; -.
DR eggNOG; COG3005; Bacteria.
DR HOGENOM; CLU_543785_0_0_7; -.
DR OMA; DTCEHCH; -.
DR Proteomes; UP000000577; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009061; P:anaerobic respiration; IBA:GO_Central.
DR Gene3D; 1.10.3820.10; -; 1.
DR InterPro; IPR036280; Multihaem_cyt_sf.
DR InterPro; IPR005126; NapC/NirT_cyt_c_N.
DR InterPro; IPR038266; NapC/NirT_cytc_sf.
DR Pfam; PF03264; Cytochrom_NNT; 1.
DR SUPFAM; SSF48695; SSF48695; 1.
DR PROSITE; PS51008; MULTIHEME_CYTC; 1.
PE 2: Evidence at transcript level;
KW Cell inner membrane; Cell membrane; Electron transport; Heme; Iron;
KW Membrane; Metal-binding; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..507
FT /note="Cytochrome c-type protein ImcH"
FT /id="PRO_0000444695"
FT TRANSMEM 14..34
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 45..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 132
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 136
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 140
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 152
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 157
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 160
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 161
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 400
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="1"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 449
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 452
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 453
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="3"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 487
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 490
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /note="covalent"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 491
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="4"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
FT BINDING 496
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_label="2"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250|UniProtKB:Q72EF4"
SQ SEQUENCE 507 AA; 57386 MW; 222E0C2E5C14FC00 CRC64;
MTLRKTAGYL WNPISLIGFL LAVVATGLII AFIAMEMITG IDHPYIGLLV YFAFPGMLIL
GLILVPIGAW RVRNQRRTEV PEEVPPYPRV DFNDPHKRRL FIFFVLASVI FVLIVSVASI
LGFEFTESTT FCGELCHVVM EPEHKAWQGS PHARVKCVEC HVGPGAEWYV KAKLSGLRQV
WAVLTHSYHF PIATPIENLR PARDTCEQCH WPEKFYSGRQ RVFYHYAPNK ENTPREINML
IKIGGTPKSP HAMGIHWHIG TEVTYIARDR KRLDIPYVAV KQKDGSIVEY MDTEKPLTRE
EIAKAEKRRM DCIDCHNRPT HIYRSPAREM DEHIVSGQID AGLPYIKKVA VEILEQPYKS
KEEAHAAIEA KLPEYYAKNF PEVAKVKAAA INQAVAHVKD IYSRNFFPRM KVTWSTYPNH
IGHFYTPGCF RCHDGKHKTS TGKIISKDCN MCHEMIGQKG ENIPEGKVVK EFVHPADIGD
ALYNVNCSDC HMAAAEDSAG GEGPGKH
