ID A0A0S4LRC2_9BACT Unreviewed; 350 AA.
AC A0A0S4LRC2;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Methylamine utilization protein MauG {ECO:0000313|EMBL:CUS39226.1};
DE EC=1.-.-.- {ECO:0000313|EMBL:CUS39226.1};
GN Name=mauG {ECO:0000313|EMBL:CUS39226.1};
GN ORFNames=COMA2_70033 {ECO:0000313|EMBL:CUS39226.1};
OS Candidatus Nitrospira nitrificans.
OC Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC Nitrospira.
OX NCBI_TaxID=1742973 {ECO:0000313|EMBL:CUS39226.1, ECO:0000313|Proteomes:UP000198736};
RN [1] {ECO:0000313|Proteomes:UP000198736}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Luecker S., Luecker S.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|ARBA:ARBA00004418}.
CC -!- PTM: Binds 2 heme groups per subunit. {ECO:0000256|PIRSR:PIRSR000294-
CC 1}.
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DR EMBL; CZPZ01000034; CUS39226.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S4LRC2; -.
DR STRING; 1742973.COMA2_70033; -.
DR Proteomes; UP000198736; Unassembled WGS sequence.
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; Cytochrome c-like domain; 2.
DR InterPro; IPR009056; Cyt_c-like_dom.
DR InterPro; IPR036909; Cyt_c-like_dom_sf.
DR InterPro; IPR004852; Di-haem_cyt_c_peroxidsae.
DR InterPro; IPR026259; MauG/Cytc_peroxidase.
DR PANTHER; PTHR30600; CYTOCHROME C PEROXIDASE-RELATED; 1.
DR PANTHER; PTHR30600:SF10; METHYLAMINE UTILIZATION PROTEIN; 1.
DR Pfam; PF03150; CCP_MauG; 1.
DR PIRSF; PIRSF000294; Cytochrome-c_peroxidase; 1.
DR SUPFAM; SSF46626; Cytochrome c; 2.
DR PROSITE; PS51007; CYTC; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR000294-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR000294-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000294-2};
KW Oxidoreductase {ECO:0000313|EMBL:CUS39226.1};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Reference proteome {ECO:0000313|Proteomes:UP000198736};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 212..335
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 80
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 83
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 84
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 227
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 230
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 231
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 350 AA; 39089 MW; DB87641C0C7929E9 CRC64;
MKRWRLTNSI PVRACMVLGL LLGFSFGEAQ AEEYKLKIPF GLEETAVAIP ADNPLTKEKI
ELGRLLFFDK RLSQDNTIAC ANCHIAKFAF TDGKPVSTGI RGQKGGRSAP ASFNRVFSSA
QFWDGRAATL EAQSVGPFTN PIEHGFVNYD VMNAKMMKIP GYRKLFKQVF GDDTITTERV
GMAIASFQRT VLSGNSPADR FDQGGETGAI SETAQRGLIL FREKARCTKC HSGFNFSDEK
FHNLGIGWDN NTVDLGRYMV TQNPEELGAF KTPTLREIAR SAPYMHDGRF KTLEEVVDFY
NKGGVKNPHQ DNLVIPLELT EQEKHDLVEF LHTLNGEGWQ HVMAPKAFPK
//
