ID B0SQ34_LEPBP Unreviewed; 401 AA.
AC B0SQ34;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 88.
DE SubName: Full=Putative cytochrome c peroxidase putative signal peptide {ECO:0000313|EMBL:ABZ99186.1};
DE EC=1.11.1.- {ECO:0000313|EMBL:ABZ99186.1};
GN OrderedLocusNames=LEPBI_I3120 {ECO:0000313|EMBL:ABZ99186.1};
OS Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris).
OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC Leptospira.
OX NCBI_TaxID=456481 {ECO:0000313|EMBL:ABZ99186.1, ECO:0000313|Proteomes:UP000001847};
RN [1] {ECO:0000313|EMBL:ABZ99186.1, ECO:0000313|Proteomes:UP000001847}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Patoc 1 / ATCC 23582 / Paris
RC {ECO:0000313|Proteomes:UP000001847};
RX PubMed=18270594; DOI=10.1371/journal.pone.0001607;
RA Picardeau M., Bulach D.M., Bouchier C., Zuerner R.L., Zidane N.,
RA Wilson P.J., Creno S., Kuczek E.S., Bommezzadri S., Davis J.C., McGrath A.,
RA Johnson M.J., Boursaux-Eude C., Seemann T., Rouy Z., Coppel R.L.,
RA Rood J.I., Lajus A., Davies J.K., Medigue C., Adler B.;
RT "Genome sequence of the saprophyte Leptospira biflexa provides insights
RT into the evolution of Leptospira and the pathogenesis of leptospirosis.";
RL PLoS ONE 3:E1607-E1607(2008).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR000294-1};
CC Note=Binds 2 heme groups. {ECO:0000256|PIRSR:PIRSR000294-1};
CC -!- PTM: Binds 2 heme groups per subunit. {ECO:0000256|PIRSR:PIRSR000294-
CC 1}.
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DR EMBL; CP000786; ABZ99186.1; -; Genomic_DNA.
DR RefSeq; WP_012390044.1; NC_010602.1.
DR AlphaFoldDB; B0SQ34; -.
DR STRING; 456481.LEPBI_I3120; -.
DR KEGG; lbi:LEPBI_I3120; -.
DR HOGENOM; CLU_034652_3_1_12; -.
DR OrthoDB; 9805202at2; -.
DR BioCyc; LBIF456481:LEPBI_RS15275-MONOMER; -.
DR Proteomes; UP000001847; Chromosome I.
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 GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.760.10; Cytochrome c-like domain; 2.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR004852; Di-haem_cyt_c_peroxidsae.
DR InterPro; IPR023929; Di-heme_enz_MXAN0977.
DR InterPro; IPR026259; MauG/Cytc_peroxidase.
DR NCBIfam; TIGR04039; MXAN_0977_Heme2; 1.
DR PANTHER; PTHR30600:SF12; BLL6722 PROTEIN; 1.
DR PANTHER; PTHR30600; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR Pfam; PF03150; CCP_MauG; 1.
DR PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1.
DR SUPFAM; SSF46626; Cytochrome c; 2.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|PIRSR:PIRSR000294-1};
KW Iron {ECO:0000256|PIRSR:PIRSR000294-2};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000294-2};
KW Oxidoreductase {ECO:0000313|EMBL:ABZ99186.1};
KW Peroxidase {ECO:0000313|EMBL:ABZ99186.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001847}.
FT DOMAIN 67..217
FT /note="Di-haem cytochrome c peroxidase"
FT /evidence="ECO:0000259|Pfam:PF03150"
FT BINDING 90
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT BINDING 93
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="1"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT BINDING 94
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:0000256|PIRSR:PIRSR000294-2"
FT BINDING 242
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT BINDING 245
FT /ligand="heme c"
FT /ligand_id="ChEBI:CHEBI:61717"
FT /ligand_label="2"
FT /note="covalent"
FT /evidence="ECO:0000256|PIRSR:PIRSR000294-1"
FT BINDING 246
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:0000256|PIRSR:PIRSR000294-2"
FT BINDING 332
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:0000256|PIRSR:PIRSR000294-2"
SQ SEQUENCE 401 AA; 44315 MW; 90702667944DF009 CRC64;
MNFMKLRISL LSVLMIGCSI LPFQKEESNN DLLLAALGIL ATASDWVWDL PPGFPVPNVP
SDNPMTKAKV ELGRHLFNEK VLSGDETMSC GSCHIQSLAF ADGKDFPTGI TNDAHPRNSQ
HLSNVAYLPR LTWSNPKMSS LEIQARAPMF GESPIELGLS SNAFLDKLKS KSIYKTLFAN
AYGNAETAVN EQNVRFAIAS FQRSMISGNS KYDQYAFRNN KSALNASEIR GLNLFNGEVA
ECFHCHGGFN FTDTSFHGGA QEEFFYHSNG IHDDAYYAAR PSNKRGLYDL TGIAADTGKF
RAPSLRNIGV TYPYMHDGSF MCDDANNPNI TMGKTKTDCA RDALTKVVDH YRSGGQNHSG
KDATLIRAFT ITNSQRDDMV NFLLTLTDDE FLTNPKFASP F
//
