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Database: UniProt
Entry: B4UHN5_ANASK
LinkDB: B4UHN5_ANASK
Original site: B4UHN5_ANASK 
ID   B4UHN5_ANASK            Unreviewed;       807 AA.
AC   B4UHN5;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:ACG72470.1};
GN   OrderedLocusNames=AnaeK_1237 {ECO:0000313|EMBL:ACG72470.1};
OS   Anaeromyxobacter sp. (strain K).
OC   Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC   Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=447217 {ECO:0000313|EMBL:ACG72470.1, ECO:0000313|Proteomes:UP000001871};
RN   [1] {ECO:0000313|EMBL:ACG72470.1, ECO:0000313|Proteomes:UP000001871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K {ECO:0000313|EMBL:ACG72470.1,
RC   ECO:0000313|Proteomes:UP000001871};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikiva G.,
RA   Beliaev A.;
RT   "Complete sequence of Anaeromyxobacter sp. K.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP001131; ACG72470.1; -; Genomic_DNA.
DR   RefSeq; WP_012525294.1; NC_011145.1.
DR   AlphaFoldDB; B4UHN5; -.
DR   KEGG; ank:AnaeK_1237; -.
DR   HOGENOM; CLU_001771_0_3_7; -.
DR   OrthoDB; 9759222at2; -.
DR   Proteomes; UP000001871; Chromosome.
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   CDD; cd00371; HMA; 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; IPR021993; ATPase-cat-bd.
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   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 2.
DR   PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR   PANTHER; PTHR43520:SF5; CATION-TRANSPORTING P-TYPE ATPASE-RELATED; 1.
DR   Pfam; PF12156; ATPase-cat_bd; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00403; HMA; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 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; 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   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW   Metal-binding {ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
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        164..183
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        203..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        417..438
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        450..472
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        760..777
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          80..146
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   807 AA;  84496 MW;  45B862FD01F8BD87 CRC64;
     MRCDHCLLEF PEREAVRAEV AGAPKVFCCA GCRGVFELIQ GEGLGAYYDS RRWTEVGPQA
     AAALDLAAFR EAVREGHGAA ELDVAIDGIR CASCVWLNEK LLQRTPGVLS ARVNYATHRA
     RIRFDPAAVG LERVLGRIQA AGYQPKPWSD AEQLRARRAE AKDLLVRLGT ALFLASQLMI
     YQAALYAGYF QGIDASTRRL MEWISLGLAL PVVFYSGAPF LRATWRGLRH LRFNMDSLVV
     IGSLAALAYS VHGMLRGGEV YFDTAAMIPT LVLVGRYVEA AAKGRASEAV ARLASLAPRE
     ARRLERGPGG RAERRSVPVA EIRPGDRIEV IPGERIPLDG VVREGASEVD ESLVTGESRP
     VAKGAGAAVI GGTVNQHGAL VVEVTRVGKD TVLAGIVRAV EEAQAQKPRI QAVADRVVGG
     FVPAMLVLAA LTVAAWLARG APVERALMTG ISVVVIACPC ALGLATPIAV LVSTGLASAR
     GLLVKGGDVV ERAGRATDVL LDKTGTVTRG RPALRALVPL DPSVGADEAL ALAAAVERRS
     EHHVGRAVAE AARALPAGAE PEAAGFRAVP GRGVIAQVGG AEVLVGNRAL LAERGVALAP
     EADARARALE AHGDTVAFLA RGGRALALVA VADPIREEAP AAIAALRALG LRVAIVSGDG
     RVTTGAVAAA LGVEAVAEAS PVEKREAVAA RQRAGRRVLF AGDGINDAPA LTQAEVGAAM
     GRGADVTMES ADAVLVRDDL RLLPDLVRLS RRTYAVIRQN VFWAFFYNAV AIPLAMAGLL
     HPIVAAGAMA ASSLFVVGNS ARLRRAL
//
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