ID X2HWG8_HELPX Unreviewed; 350 AA.
AC X2HWG8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Cytochrome C biogenesis protein CcsA {ECO:0000313|EMBL:AHN36820.1};
GN ORFNames=HPOKI112_07400 {ECO:0000313|EMBL:AHN36820.1};
OS Helicobacter pylori oki112.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1382921 {ECO:0000313|EMBL:AHN36820.1, ECO:0000313|Proteomes:UP000019647};
RN [1] {ECO:0000313|EMBL:AHN36820.1, ECO:0000313|Proteomes:UP000019647}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oki112 {ECO:0000313|EMBL:AHN36820.1};
RX PubMed=24744331;
RA Satou K., Shiroma A., Teruya K., Shimoji M., Nakano K., Juan A.,
RA Tamotsu H., Terabayashi Y., Aoyama M., Teruya M., Suzuki R., Matsuda M.,
RA Sekine A., Kinjo N., Kinjo F., Yamaoka Y., Hirano T.;
RT "Complete Genome Sequences of Eight Helicobacter pylori Strains with
RT Different Virulence Factor Genotypes and Methylation Profiles, Isolated
RT from Patients with Diverse Gastrointestinal Diseases on Okinawa Island,
RT Japan, Determined Using PacBio Single-Molecule Real-Time Technology.";
RL Genome Announc. 2:e00286-14(2014).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP006821; AHN36820.1; -; Genomic_DNA.
DR RefSeq; WP_025276421.1; NZ_CP006821.1.
DR AlphaFoldDB; X2HWG8; -.
DR KEGG; hpyc:HPOKI112_07400; -.
DR HOGENOM; CLU_034652_1_0_7; -.
DR Proteomes; UP000019647; Chromosome.
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:SF7; 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; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Periplasm {ECO:0000256|ARBA:ARBA00022764};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..350
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004950309"
FT DOMAIN 220..327
FT /note="Cytochrome c"
FT /evidence="ECO:0000259|PROSITE:PS51007"
FT BINDING 88
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 91
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 92
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 234
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 237
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 238
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 302
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; 38833 MW; 5797F5CE2719CC56 CRC64;
MKKSVLLGVC LAFSCTHALS DMDLIKKARE SQLEPMPMGK ALKEYQIKKT RDVGIGTKNS
EIMTSAQVEL GKMLYFDPRI STSYLVSCNT CHNLGLGGVD LVPSAIGSQW KKNPHLLSSP
TVYNSVFNDV QFWDGRVTHL NEQAQGPIQS SFEMGADPKV VVEKINSMPG YVKLFRKAYG
SKVKIDFKLI ADSIAMFEAT LITPSRYDDF LRGNPKALSK AEKEGLNLFI SKGCVACHNG
INLGGTMQPF GVVKPYKFAN VGDFKGDKNG LVKVPTLRNI TETMPYFHNG QFWDVKDAIK
EMGSIQLGIE ISDEEAKKIE IFFEALKGKK PKILYPELPV MTDKTPKPSF
//
