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Database: UniProt
Entry: Q21AR2_RHOPB
LinkDB: Q21AR2_RHOPB
Original site: Q21AR2_RHOPB 
ID   Q21AR2_RHOPB            Unreviewed;       212 AA.
AC   Q21AR2;
DT   18-APR-2006, integrated into UniProtKB/TrEMBL.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   RecName: Full=Cytochrome c-type protein {ECO:0000256|PIRNR:PIRNR000013};
GN   OrderedLocusNames=RPC_0954 {ECO:0000313|EMBL:ABD86524.1};
OS   Rhodopseudomonas palustris (strain BisB18).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Rhodopseudomonas.
OX   NCBI_TaxID=316056 {ECO:0000313|EMBL:ABD86524.1};
RN   [1] {ECO:0000313|EMBL:ABD86524.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB18 {ECO:0000313|EMBL:ABD86524.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL   Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000013-1};
CC       Note=Binds 4 heme groups per subunit. {ECO:0000256|PIRSR:PIRSR000013-
CC       1};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- PTM: Binds 4 heme groups per subunit. {ECO:0000256|PIRNR:PIRNR000013}.
CC   -!- SIMILARITY: Belongs to the NapC/NirT/NrfH family.
CC       {ECO:0000256|ARBA:ARBA00007395}.
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DR   EMBL; CP000301; ABD86524.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q21AR2; -.
DR   STRING; 316056.RPC_0954; -.
DR   KEGG; rpc:RPC_0954; -.
DR   eggNOG; COG3005; Bacteria.
DR   HOGENOM; CLU_096753_2_0_5; -.
DR   OrthoDB; 7360653at2; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019333; P:denitrification pathway; IEA:InterPro.
DR   Gene3D; 1.10.3820.10; Di-heme elbow motif domain; 1.
DR   InterPro; IPR036280; Multihaem_cyt_sf.
DR   InterPro; IPR024717; NapC/NirT/NrfH.
DR   InterPro; IPR005126; NapC/NirT_cyt_c_N.
DR   InterPro; IPR038266; NapC/NirT_cytc_sf.
DR   InterPro; IPR011885; NO3Rdtase_cyt_c_NapC/NirT.
DR   NCBIfam; TIGR02161; napC_nirT; 1.
DR   PANTHER; PTHR30333; CYTOCHROME C-TYPE PROTEIN; 1.
DR   PANTHER; PTHR30333:SF1; CYTOCHROME C-TYPE PROTEIN NAPC; 1.
DR   Pfam; PF03264; Cytochrom_NNT; 1.
DR   PIRSF; PIRSF000013; 4_hem_cytochrm_NapC; 1.
DR   SUPFAM; SSF48695; Multiheme cytochromes; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW   ECO:0000256|PIRNR:PIRNR000013};
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR000013};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR000013};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR000013};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000013}.
FT   TRANSMEM        34..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          31..205
FT                   /note="NapC/NirT cytochrome c N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF03264"
FT   BINDING         68
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT   BINDING         71
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT   BINDING         74
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:0000256|PIRSR:PIRSR000013-2"
FT   BINDING         98
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT   BINDING         101
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT   BINDING         102
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:0000256|PIRSR:PIRSR000013-2"
FT   BINDING         120
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:0000256|PIRSR:PIRSR000013-2"
FT   BINDING         158
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="3"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT   BINDING         161
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="3"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT   BINDING         162
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:0000256|PIRSR:PIRSR000013-2"
FT   BINDING         191
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="4"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT   BINDING         194
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_label="4"
FT                   /note="covalent"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000013-1"
FT   BINDING         195
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:0000256|PIRSR:PIRSR000013-2"
FT   BINDING         200
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:0000256|PIRSR:PIRSR000013-2"
SQ   SEQUENCE   212 AA;  24021 MW;  14BFE38C92EBABA4 CRC64;
     MTAIDPSAPR RSWLARAWQF LKDLWQVLLR PSSVFGLGVL VLAGFVAGIV FWGGFNTVLE
     ATNTEKFCTG CHEMRDNVFA ELKPTIHFSN RSGVRASCPD CHVPHNWTDK IARKMQASKE
     VWGHLFGSID TPDKFRENRL ELAMHEWSRF KANDSLECRN CHSAASMDIT KQSPRASVAH
     QRYLFTGEKT CIDCHKGIAH HLPDMRGVPG WQ
//
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