ID Q8P7E9_XANCP Unreviewed; 457 AA.
AC Q8P7E9;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=Cytochrome D oxidase subunit A {ECO:0000313|EMBL:AAM41934.1};
GN Name=qxtA {ECO:0000313|EMBL:AAM41934.1};
GN OrderedLocusNames=XCC2662 {ECO:0000313|EMBL:AAM41934.1};
OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS 528 / LMG 568 / P 25).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190485 {ECO:0000313|EMBL:AAM41934.1, ECO:0000313|Proteomes:UP000001010};
RN [1] {ECO:0000313|EMBL:AAM41934.1, ECO:0000313|Proteomes:UP000001010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25
RC {ECO:0000313|Proteomes:UP000001010};
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F.Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P.Jr., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A.Jr., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|PIRNR:PIRNR006446}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the cytochrome ubiquinol oxidase subunit 1
CC family. {ECO:0000256|ARBA:ARBA00009819, ECO:0000256|PIRNR:PIRNR006446}.
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DR EMBL; AE008922; AAM41934.1; -; Genomic_DNA.
DR RefSeq; NP_638010.1; NC_003902.1.
DR RefSeq; WP_011037792.1; NC_003902.1.
DR AlphaFoldDB; Q8P7E9; -.
DR STRING; 190485.XCC2662; -.
DR EnsemblBacteria; AAM41934; AAM41934; XCC2662.
DR KEGG; xcc:XCC2662; -.
DR PATRIC; fig|190485.4.peg.2838; -.
DR eggNOG; COG1271; Bacteria.
DR HOGENOM; CLU_030555_3_1_6; -.
DR OrthoDB; 9807042at2; -.
DR Proteomes; UP000001010; Chromosome.
DR GO; GO:0070069; C:cytochrome complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0009055; F:electron transfer activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016682; F:oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor; IBA:GO_Central.
DR GO; GO:0019646; P:aerobic electron transport chain; IBA:GO_Central.
DR InterPro; IPR002585; Cyt-d_ubiquinol_oxidase_su_1.
DR PANTHER; PTHR30365:SF14; CYTOCHROME BD2 SUBUNIT I; 1.
DR PANTHER; PTHR30365; CYTOCHROME D UBIQUINOL OXIDASE; 1.
DR Pfam; PF01654; Cyt_bd_oxida_I; 1.
DR PIRSF; PIRSF006446; Cyt_quinol_oxidase_1; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|PIRNR:PIRNR006446};
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR006446};
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR006446};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR006446};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR006446};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR006446};
KW Reference proteome {ECO:0000313|Proteomes:UP000001010};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|PIRNR:PIRNR006446};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|PIRNR:PIRNR006446};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR006446}.
FT TRANSMEM 15..43
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 55..74
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 94..116
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 187..208
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 220..239
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 324..348
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 360..382
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
FT TRANSMEM 415..436
FT /note="Helical"
FT /evidence="ECO:0000256|PIRNR:PIRNR006446"
SQ SEQUENCE 457 AA; 50388 MW; 343F1139BEC1FDF2 CRC64;
MQASEHALLL VRGQFAFTIG MHIVLAAFTM GLANFLVVLE ALWLRTRRRV YMDVYNYWLK
LFSLTTAAGV VTGIPMEFVF GLHWGRLSGA AGAVIGPLMF FEVLVAFFLE AGFLGIMLFG
MKKVGHRVHF FATCMVALGS LVSAFWILSA NSWLHTPAGF ARAADGNFLP VDWLRIIFNP
SFPWRMLHMS LAALLATAAI IAAVGAWHVL RDTRNPGARL MFSMGLWVIA IVAPLQLLAG
DLHGRNTLEH QPQKLAAIEG SWQRPPAGEG EPLRLFAIPD MQAQRNRHEL AIPRLGSLYL
RHNWTGTIAG LREFPRSDLP PVPIVFFAFR AMVGLGLLLI AVGMLSLVLR ARGRLYEARW
LQRVVVVMAP SGMLAMLCGW VVTEVGRQPF TVYGLLRTAH STSPLSLPMV ASSSVAILVL
YPLVFGLGLF LLLRVLRRLP HARERGPSPG LADQTGN
//
