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Database: UniProt
Entry: A0A1V0GZ48_9RHOB
LinkDB: A0A1V0GZ48_9RHOB
Original site: A0A1V0GZ48_9RHOB 
ID   A0A1V0GZ48_9RHOB        Unreviewed;       395 AA.
AC   A0A1V0GZ48;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 2.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Methylamine utilization protein MauG {ECO:0000313|EMBL:ARC39060.2};
GN   ORFNames=A6J80_22025 {ECO:0000313|EMBL:ARC39060.2};
OS   Paracoccus yeei.
OG   Plasmid unnamed5 {ECO:0000313|EMBL:ARC39060.2,
OG   ECO:0000313|Proteomes:UP000191257}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=147645 {ECO:0000313|EMBL:ARC39060.2, ECO:0000313|Proteomes:UP000191257};
RN   [1] {ECO:0000313|Proteomes:UP000191257}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FDAARGOS_252 {ECO:0000313|Proteomes:UP000191257};
RC   PLASMID=Plasmid unnamed5 {ECO:0000313|Proteomes:UP000191257};
RA   Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA   Sadzewicz L., Sengamalay N., Ott S., Godinez A., Nagaraj S., Nadendla S.,
RA   Geyer C., Sichtig H.;
RT   "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT   Supporting development and validation of Infectious Disease Dx tests.";
RL   Submitted (MAR-2017) 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; CP020445; ARC39060.2; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V0GZ48; -.
DR   KEGG; pye:A6J80_22025; -.
DR   eggNOG; COG1858; Bacteria.
DR   Proteomes; UP000191257; Plasmid unnamed5.
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: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; PS51007; CYTC; 2.
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   Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW   Plasmid {ECO:0000313|EMBL:ARC39060.2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191257};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..395
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015114122"
FT   DOMAIN          37..195
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   DOMAIN          215..378
FT                   /note="Cytochrome c"
FT                   /evidence="ECO:0000259|PROSITE:PS51007"
FT   BINDING         59
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         62
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         63
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         229
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         232
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         233
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   395 AA;  43179 MW;  1BB5DB3AF670FB77 CRC64;
     MTGRLPSRLL VLAIPLAGAV LVGAAAGRQP APPAPGDLAA LGQRLFHDTA LSRTGTQSCA
     TCHDPEHAFT DPREGAAGRA VSLGDDGVSY GDRNTPTLSY AALSPDFHRD DKGRYKGGQF
     WDGRADDLAD QAGQPMLNPV EMGMPDKAAV VERLRADPGY AQDFAVLFGP QALGDVDRAF
     DHAAEALAAY QRTETFMPFD SRYDRFLRGE EELTAQERFG HTVFITWNCR LCHQLQKQGI
     VERETFTSFE YHNIGVPVNR AARDANGLGP DHLDLGLLDR PGIDDPAQAG RMKVPTLRNV
     AVTGPYMHNG AFSDLRTAVL FYNKYTSRRP GSQINPETGE DWGPAEIDRN LSLTELQSGL
     MLDDARVDAL VAFLETLTDR RYEPLLAERK RGAAD
//
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