ID   NIRC_PSEST              Reviewed;         113 AA.
AC   P24039;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 88.
DE   RecName: Full=Cytochrome c55X;
DE   Flags: Precursor;
GN   Name=nirC;
OS   Pseudomonas stutzeri (Pseudomonas perfectomarina).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 14405 / JCM 20778 / CIP 107696 / IAM 12931 / LMG 2243 / NCIMB
RC   568 / 218 / ZoBell 632;
RX   PubMed=2001732; DOI=10.1016/0014-5793(91)80150-2;
RA   Juengst A., Wakabayashi S., Matsubara H., Zumft W.G.;
RT   "The nirSTBM region coding for cytochrome cd1-dependent nitrite respiration
RT   of Pseudomonas stutzeri consists of a cluster of mono-, di-, and tetraheme
RT   proteins.";
RL   FEBS Lett. 279:205-209(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 103-113.
RX   PubMed=7588711; DOI=10.1111/j.1432-1033.1995.tb20868.x;
RA   Palmedo G., Seither P., Koerner H., Matthews J.C., Burkhalter R.S.,
RA   Timkovich R., Zumft W.G.;
RT   "Resolution of the nirD locus for heme d1 synthesis of cytochrome cd1
RT   (respiratory nitrite reductase) from Pseudomonas stutzeri.";
RL   Eur. J. Biochem. 232:737-746(1995).
CC   -!- FUNCTION: Monoheme c-type cytochrome. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000250}.
CC   -!- PTM: Binds 1 heme c group covalently per subunit.
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DR   EMBL; X53676; CAA40154.1; -; Genomic_DNA.
DR   PIR; S13940; CCPSS.
DR   RefSeq; WP_003279938.1; NZ_POUM01000011.1.
DR   AlphaFoldDB; P24039; -.
DR   SMR; P24039; -.
DR   STRING; 32042.PstZobell_00947; -.
DR   eggNOG; COG2010; Bacteria.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.760.10; -; 1.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   InterPro; IPR036909; Cyt_c-like_dom_sf.
DR   Pfam; PF13442; Cytochrome_CBB3; 1.
DR   SUPFAM; SSF46626; SSF46626; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   3: Inferred from homology;
KW   Electron transport; Heme; Iron; Metal-binding; Periplasm; Signal;
KW   Transport.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..113
FT                   /note="Cytochrome c55X"
FT                   /id="PRO_0000006573"
FT   BINDING         45
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         48
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         49
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
SQ   SEQUENCE   113 AA;  11924 MW;  A249222996047F67 CRC64;
     MTVARHAVSR LGLALASFLL FPLALAAAPA AERQATLDHL LLQDCGSCHG LRMTGGLGPA
     LTREALAGKP RDSLIATVTH GRPGTAMPGW NALLDEQDIA YLVDRLLEGY PKP