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Database: UniProt
Entry: C1F6K7_ACIC5
LinkDB: C1F6K7_ACIC5
Original site: C1F6K7_ACIC5 
ID   C1F6K7_ACIC5            Unreviewed;       948 AA.
AC   C1F6K7;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   SubName: Full=Cation transport ATPase (P-type) family, type IIA subfamily {ECO:0000313|EMBL:ACO32385.1};
DE            EC=3.6.3.- {ECO:0000313|EMBL:ACO32385.1};
GN   OrderedLocusNames=ACP_1509 {ECO:0000313|EMBL:ACO32385.1};
OS   Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM
OS   7670 / NBRC 15755 / NCIMB 13165 / 161).
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Acidobacterium.
OX   NCBI_TaxID=240015 {ECO:0000313|EMBL:ACO32385.1, ECO:0000313|Proteomes:UP000002207};
RN   [1] {ECO:0000313|EMBL:ACO32385.1, ECO:0000313|Proteomes:UP000002207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 /
RC   NCIMB 13165 / 161 {ECO:0000313|Proteomes:UP000002207};
RX   PubMed=19201974; DOI=10.1128/AEM.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP001472; ACO32385.1; -; Genomic_DNA.
DR   RefSeq; WP_015896641.1; NC_012483.1.
DR   AlphaFoldDB; C1F6K7; -.
DR   STRING; 240015.ACP_1509; -.
DR   KEGG; aca:ACP_1509; -.
DR   eggNOG; COG0474; Bacteria.
DR   HOGENOM; CLU_002360_3_3_0; -.
DR   InParanoid; C1F6K7; -.
DR   Proteomes; UP000002207; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR   InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR   PANTHER; PTHR42861:SF156; CALCIUM-TRANSPORTING ATPASE; 1.
DR   Pfam; PF13246; Cation_ATPase; 1.
DR   Pfam; PF00689; Cation_ATPase_C; 1.
DR   Pfam; PF00690; Cation_ATPase_N; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00120; HATPASE.
DR   SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00831; Cation_ATPase_N; 1.
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; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Hydrolase {ECO:0000313|EMBL:ACO32385.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002207};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        69..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        93..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        261..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        291..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        722..747
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        810..832
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        874..894
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        906..926
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          12..86
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   948 AA;  101181 MW;  38BA2F7E9EEB90D2 CRC64;
     MQPGVHTQSH KPPHQASPDE VRCDYATDMQ RGLRADEADR RLLQYGPNAL PHPEPPAIWF
     RLLRQLADVQ VYLLLAAAAI SLLVWSIGRE SALPLEAIAI LAIVVLNVLF GFLQEERAGR
     ASMALQQMTP HEASVLRDGK LMRIDVRRIV PGDLLLIQEG DKIAADGRLI DVTALQTQEA
     ALTGESQPIR KSIVTLPRAT GIADRSNMIF AGTVAASGHA RAIVTATGAA TELGRIGAML
     SATPDQLTPL QQELNALGKK LGAAVLIIAA VVVITLLSLQ HTLSSTIILR ALLFGIALAV
     AAIPEGLAAV ITVVLALGVR RMARRGAIVR HLKAVETLGE ATVIACDKTG TMTSNTMRVT
     CAATASGLSA LVSSHAGPSV SSTHSFKGPS TPSAQCELTL ALAAAALTNN ARLRETSTGP
     IAEGDPTEAA LLLAACEAGQ YVKDLIAACP RIMEFPFTSE RKRMSTLHHC LNHAREVFGA
     PSVLLIKGAA DLLLDRATQE AVDGHWRPLT PERKQTWRTM QNNMAADALR TLGVAIRPLP
     ALPSEGSDNA EQWERDLIFA GILGISDPPR PGVREAVAIA RAAGVRTIML TGDHAATALA
     VARALDISKD ERVITGSQLS SMSDEELGQV AVHTSVFARV DPEHKLRLVK ALRQNGDIVA
     MTGDGVNDAP ALKAADIGIA MGITGTGVAK EAADMILADD NFATIVAAIT EGKSIFKNIR
     RFLRYILACN AGEVLTLFAA VSFSSFANRG QDELVLPLLA LQILWINLIT DGAPALALGL
     EIPHLQGINI CPPPVRARIP SKTRIIDRAM LADIGIVALI IAAGTLGLFY AVAGNLELRR
     TMAFTTLILF QLFNAFEARS STQSILAGLF RNRWLWAATG AMLILQVLLL QWPAAGRIFG
     VVPLSLSHWI ECAVTASTVV WGMEAVKWLR RIRFARKDPV QLGETASH
//
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