ID A0A1N7QCX5_9RHOB Unreviewed; 622 AA.
AC A0A1N7QCX5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE SubName: Full=Cytochrome c biogenesis protein CcdA {ECO:0000313|EMBL:SIT20720.1};
GN ORFNames=SAMN05421580_11612 {ECO:0000313|EMBL:SIT20720.1};
OS Rhodobacter aestuarii.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=453582 {ECO:0000313|EMBL:SIT20720.1, ECO:0000313|Proteomes:UP000186221};
RN [1] {ECO:0000313|Proteomes:UP000186221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19945 {ECO:0000313|Proteomes:UP000186221};
RA Varghese N., Submissions S.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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; FTOG01000016; SIT20720.1; -; Genomic_DNA.
DR RefSeq; WP_076486359.1; NZ_QAXT01000014.1.
DR AlphaFoldDB; A0A1N7QCX5; -.
DR STRING; 453582.SAMN05421580_11612; -.
DR OrthoDB; 9811352at2; -.
DR Proteomes; UP000186221; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016209; F:antioxidant activity; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0017004; P:cytochrome complex assembly; IEA:InterPro.
DR CDD; cd03012; TlpA_like_DipZ_like; 1.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR000866; AhpC/TSA.
DR InterPro; IPR003834; Cyt_c_assmbl_TM_dom.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR041017; Thioredoxin_10.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR42852:SF13; PROTEIN DIPZ; 1.
DR PANTHER; PTHR42852; THIOL:DISULFIDE INTERCHANGE PROTEIN DSBE; 1.
DR Pfam; PF00578; AhpC-TSA; 1.
DR Pfam; PF02683; DsbD; 1.
DR Pfam; PF17991; Thioredoxin_10; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000186221};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 40..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 120..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 158..181
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 294..446
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
SQ SEQUENCE 622 AA; 64564 MW; 917A6A907045EB7A CRC64;
MTLALLAYLG GVLTILSPCI LPVLPFVFAR AGLSFWRGPA PMLVGMALAF AAVATLAAVG
GGWAVAANQW GRWIALALLA AFGLMLLLPG LSDRLSRPVV ALGNRLSTQA EAQPSIGGSV
LLGIATGLLW APCAGPILGL ILTGAALNGA SLGTTALLLA YALGAATALG VAAFAGGRLF
AALKRSLGFG EGLRRVLGVA VLAGVAGIAL GLDTGILTKL STASTNRLEA GLIEKLGPQE
TASVVMPEAG GAMMMQGGPA MMAGGAAMTG PAMTGGPAMT GNPALMMAAD PAMVGTGAAA
LPIEGQMPPL EGAVQWLNSD PLTAEELRGK VVLIDFWTYS CINCLRAIPY VKAWAETYGP
QGLVVIGVHA PEFAFEKDPR NVTRAANDLG ITYPVALDND YAIWRAFQNR FWPAHYFIDA
EGRIRHHHFG EGGYEESEQV IQQLLAEAGL SKVALPPTEV TGSGVSAAAN MAEVLSPETY
LGHARAANNF NAEGLVANEA HDYAAATDLR LNEWSFDGRW AVGEEAARLA GPEGAINFRF
HARDVHLVLS PGVAAKPVPF TVTIDGQPPG ADAGLDVDAE GRGTVTTDRL YQLYRAKGAV
GEHLFEIRFD HPGVEAFAFT FG
//
