ID   C552_PSEST              Reviewed;         291 AA.
AC   P24037;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-1992, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Cytochrome c-552;
DE   Flags: Precursor;
GN   Name=nirB;
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   PROTEIN SEQUENCE OF 24-270.
RC   STRAIN=ATCC 14405 / JCM 20778 / CIP 107696 / IAM 12931 / LMG 2243 / NCIMB
RC   568 / 218 / ZoBell 632;
RX   PubMed=2539041; DOI=10.1016/0003-9861(89)90013-1;
RA   Denariaz C.M., Liu M.-Y., Payne W.J., le Gall J., Marquez L., Dunford H.B.,
RA   van Beeumen J.;
RT   "Cytochrome c peroxidase activity of a protease-modified form of cytochrome
RT   c-552 from the denitrifying bacterium Pseudomonas perfectomarina.";
RL   Arch. Biochem. Biophys. 270:114-125(1989).
CC   -!- FUNCTION: May play a role in nitrite reduction. Shows peroxidase
CC       activity on proteolytic modification.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- INDUCTION: By anaerobic conditions.
CC   -!- PTM: Binds 2 heme c groups per subunit.
CC   -!- MISCELLANEOUS: The second heme binding site has an unusual CXXXCH
CC       motif.
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DR   EMBL; X53676; CAA40152.1; -; Genomic_DNA.
DR   PIR; S13938; CCPS2S.
DR   RefSeq; WP_003279941.1; NZ_POUM01000011.1.
DR   AlphaFoldDB; P24037; -.
DR   STRING; 32042.PstZobell_00957; -.
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   InterPro; IPR019020; Cyt-c552/DMSO_Rdtase_haem-bd.
DR   InterPro; IPR009056; Cyt_c-like_dom.
DR   Pfam; PF09459; EB_dh; 2.
DR   SMART; SM00887; EB_dh; 1.
DR   PROSITE; PS51007; CYTC; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Electron transport; Heme; Iron; Metal-binding;
KW   Periplasm; Repeat; Signal; Transport.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000269|PubMed:2539041"
FT   CHAIN           24..291
FT                   /note="Cytochrome c-552"
FT                   /evidence="ECO:0000269|PubMed:2001732"
FT                   /id="PRO_0000006570"
FT   BINDING         68
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         71
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         72
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="1"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         157
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         161
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   BINDING         162
FT                   /ligand="heme c"
FT                   /ligand_id="ChEBI:CHEBI:61717"
FT                   /ligand_label="2"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00433"
FT   CONFLICT        59
FT                   /note="A -> D (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        229
FT                   /note="D -> N (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        268..270
FT                   /note="RYH -> SYN (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   291 AA;  30426 MW;  DB34BC903CD2687F CRC64;
     MKKTLMASAV GAVIAFGTHG AMAAAPADWS SVAATDVTLF YPGVSPVEWI TKGTEHGGAR
     ALKKGETCAG CHSEEASDMG EKMASGKKLE PSPIAGKAPF INAKVQAAND GENLYLRFTW
     KQPAASGAAP MDADNPVKIA YMLEGGSKVE LAEAGGCWGS CHGDARTMPG AADTKTKYVK
     DGSLANGVYY DLNQWRSGEN KAFDGYVATE RVMEGGQALV DAQGKLDGDT WTVVFTRKFA
     GGEGDVTLAP GNLYNFGFAI HDDSATGRYH HVSLGYSLGI DAQGDITAAK Q