ID Q8YFF3_BRUME Unreviewed; 752 AA.
AC Q8YFF3; D0B575;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 161.
DE SubName: Full=Nitrogen fixation protein fixi (E1-e2 type cation atpase fixi) {ECO:0000313|EMBL:AAL52750.1};
DE EC=3.6.1.- {ECO:0000313|EMBL:AAL52750.1};
GN OrderedLocusNames=BMEI1569 {ECO:0000313|EMBL:AAL52750.1};
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914 {ECO:0000313|EMBL:AAL52750.1, ECO:0000313|Proteomes:UP000000419};
RN [1] {ECO:0000313|EMBL:AAL52750.1, ECO:0000313|Proteomes:UP000000419}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094
RC {ECO:0000313|Proteomes:UP000000419};
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.J.,
RA Haselkorn R., Kyrpides N., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC ECO:0000256|RuleBase:RU362081}.
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; AE008917; AAL52750.1; -; Genomic_DNA.
DR PIR; AC3448; AC3448.
DR RefSeq; WP_004682969.1; NZ_GG703778.1.
DR AlphaFoldDB; Q8YFF3; -.
DR GeneID; 29594416; -.
DR KEGG; bme:BMEI1569; -.
DR KEGG; bmel:DK63_1923; -.
DR PATRIC; fig|224914.52.peg.2024; -.
DR eggNOG; COG2217; Bacteria.
DR Proteomes; UP000000419; Chromosome I.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd00371; HMA; 1.
DR CDD; cd02092; P-type_ATPase_FixI-like; 1.
DR Gene3D; 3.30.70.100; -; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR InterPro; IPR018303; ATPase_P-typ_P_site.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01512; ATPase-IB2_Cd; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF5; CATION-TRANSPORTING P-TYPE ATPASE-RELATED; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Hydrolase {ECO:0000313|EMBL:AAL52750.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 114..135
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 179..201
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 207..225
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 363..385
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 391..417
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 686..705
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 711..728
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 34..99
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 752 AA; 81009 MW; D77427587B9114AA CRC64;
MSCCVENAQI ATVIQSVSPE EMQIASRALG DGLRQLDLSV PGVHCGLCIK TIEDALGKIS
GVAYVRVNLT ARRVTLRWKD GETPPNVVDT LRRLGYEAHI FDMAQDKDPT FTRLLIALGV
AAFASSNVML LSVAVWSGAD AATRDMFHWI SGLIAFPTLV YSGRIFYVSA WNALRAGNVN
MDVPIALAIS LAFAMSVYET IHHGQHAYFD ASVTLLFFLL IGRTLDYMMR ARARSAVRGL
AQLGSRGAVV IGENDERNYL PVNEIRPGMR IILAAGERVP VDAKVEEGRS ELDCSIASGE
SDAVPVGPGS DIRAGTLNLS TPLVIRATAE ARDSFLSEMV RLMDVAEDGR AHYRRLADRA
SELYVPMVHA TAFLALAGWM FYTGGDWYRS IYIAISTLII TCPCALALAV PIVQVVAARR
LFENGIMIKD GSAMERMAEI DTAVFDKTGT LTLGQPWLIN AQEIEPHYLE IAAELSLYSR
HPLSRALALF SGATPMTPFT RIEEVPGAGI EAELDGTIYR LGKQEWACGK AETAQPSGPE
TCLSIDGRLV QVFRFEDRPR EDAANAIAAL KRNGLKLGII SGDKQAAVKK LADYLGVNDY
HSGVLPADKS KLVQELSSEG RKVLMVGDGL NDAPALVAAH VSMAPATAAD IGRNAADFVF
LRESLSAVPL AFAVSKEAGK LVSQNFGLSI GYNIIAVPIA VFGYVTPLVA ALSMSLSSIV
VVTNALRLRA GKQKQQARQS GAPATTMKEA HK
//
