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Database: UniProt
Entry: A2TX00_9FLAO
LinkDB: A2TX00_9FLAO
Original site: A2TX00_9FLAO 
ID   A2TX00_9FLAO            Unreviewed;       651 AA.
AC   A2TX00;
DT   20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   20-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 95.
DE   SubName: Full=Putative zinc-transporting P-type ATPase {ECO:0000313|EMBL:EAQ41079.1};
DE            EC=3.6.3.5 {ECO:0000313|EMBL:EAQ41079.1};
GN   ORFNames=MED152_00155 {ECO:0000313|EMBL:EAQ41079.1};
OS   Polaribacter sp. MED152.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=313598 {ECO:0000313|EMBL:EAQ41079.1, ECO:0000313|Proteomes:UP000006470};
RN   [1] {ECO:0000313|EMBL:EAQ41079.1, ECO:0000313|Proteomes:UP000006470}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MED152 {ECO:0000313|EMBL:EAQ41079.1};
RX   PubMed=17215843; DOI=10.1038/nature05381;
RA   Gomez-Consarnau L., Gonzalez J.M., Coll-Llado M., Gourdon P., Pascher T.,
RA   Neutze R., Pedros-Alio C., Pinhassi J.;
RT   "Light stimulates growth of proteorhodopsin-containing marine
RT   Flavobacteria.";
RL   Nature 445:210-213(2007).
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; CP004349; EAQ41079.1; -; Genomic_DNA.
DR   RefSeq; WP_015479811.1; NC_020830.1.
DR   AlphaFoldDB; A2TX00; -.
DR   STRING; 313598.MED152_00155; -.
DR   KEGG; pom:MED152_00155; -.
DR   eggNOG; COG2217; Bacteria.
DR   HOGENOM; CLU_001771_6_2_10; -.
DR   OrthoDB; 1521937at2; -.
DR   Proteomes; UP000006470; 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   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; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01512; ATPase-IB2_Cd; 1.
DR   NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR48085; CADMIUM/ZINC-TRANSPORTING ATPASE HMA2-RELATED; 1.
DR   PANTHER; PTHR48085:SF5; CADMIUM_ZINC-TRANSPORTING ATPASE HMA2; 1.
DR   Pfam; PF00122; E1-E2_ATPase; 1.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00941; CDATPASE.
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   PROSITE; PS00154; ATPASE_E1_E2; 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:EAQ41079.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000006470};
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        38..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        65..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        95..113
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        119..136
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        300..321
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        598..618
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        624..643
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
SQ   SEQUENCE   651 AA;  71566 MW;  853940B911F917F4 CRC64;
     MKKKKINLKD LKPVSKEEHN HDNGHNHDHQ ESGSFKTYIP AIISFTMLII GIGLDYFDVS
     FFRDWIRIAW YSLAYLPVGF PVVREGWNSI KKGDVFTEFF LMSIATIGAF IIGEYPEGVA
     VMLFYAVGEL FQNAAVNRAK GNIKALLDVR PKEANVFRDG DYVSVSPEAV NIGEKIQIRV
     GEKIPLDGKL LSSKASLNTS ALTGESKPDT IVKDEKVYAG SINLESVIEV EVTNKFEDSS
     IARILDLVQN ATARKSKTEL FIRQFARIYT PIVVFLAIGV TFIPYFFVDD YVFRDWLYRA
     LIFLVISCPC ALVISIPLGY FGGLGAASKN GILFKGASFL DAMTKINTLV MDKTGTVTKG
     VFKIKKVQAF GWNEAEFMQY LMAMEELSTH PIAKAILEYK AEGEYFEAKE VSEIAGKGLK
     GIVNDKTVLV GNKALMSANN INVPKETESI LESIVLVAID NQFAGYVVIA DELKEDAKET
     ITNLHKVGIK NIMMLSGDKD SITQQVAKEL NIANAKGGLL PEDKLKEVEI LKKNPENKIA
     FIGDGINDAP VLAASNVGIA MGGLGSDVAI ETADVIIQTD QPSKVVRAIK ISRSTRKIVW
     QNIILAFGVK VIVLILGAGG LATMWEAVFA DVGVALLAIL NAVRLQRMIW D
//
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