ID C0Q9Q0_DESAH Unreviewed; 794 AA.
AC C0Q9Q0;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 89.
DE SubName: Full=ZntA {ECO:0000313|EMBL:ACN14614.1};
DE EC=3.6.3.4 {ECO:0000313|EMBL:ACN14614.1};
GN Name=zntA {ECO:0000313|EMBL:ACN14614.1};
GN OrderedLocusNames=HRM2_15050 {ECO:0000313|EMBL:ACN14614.1};
OS Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS HRM2) (Desulfobacterium autotrophicum).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfobacteraceae; Desulforapulum.
OX NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN14614.1, ECO:0000313|Proteomes:UP000000442};
RN [1] {ECO:0000313|EMBL:ACN14614.1, ECO:0000313|Proteomes:UP000000442}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC {ECO:0000313|Proteomes:UP000000442};
RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA Meyerdierks A., Gottschalk G., Amann R.;
RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT reducer oxidizing organic carbon completely to carbon dioxide.";
RL Environ. Microbiol. 11:1038-1055(2009).
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; CP001087; ACN14614.1; -; Genomic_DNA.
DR AlphaFoldDB; C0Q9Q0; -.
DR STRING; 177437.HRM2_15050; -.
DR KEGG; dat:HRM2_15050; -.
DR eggNOG; COG2217; Bacteria.
DR eggNOG; COG2608; Bacteria.
DR HOGENOM; CLU_001771_0_3_7; -.
DR Proteomes; UP000000442; 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; 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; 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:ACN14614.1};
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:UP000000442};
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 149..170
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 209..231
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 399..421
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 433..459
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 741..760
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 766..784
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 70..136
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 36..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 794 AA; 86361 MW; 93CC3377D65636F3 CRC64;
MVHAMLMESD EYKDTKDFKD TDLYKQCVAA GIVPDTTKET SESWEARLEP PAPELSGTDS
EVPMDAGNFL TLNLQIQNMW CPACAWLIET TLTRSKGVVN ASCNFSSDRG SVVYDPVKTS
PDKIYAAIEK LGYPAADINQ KASKSRAEFI RICVTLFLTM NVMMLSWSIY SGFFIELSPH
AVQLLAWPVF LMATVVVFYG GYPIHKRALA GITSGFPGME TLVSTGSFST YTYSLFHFYR
GSIHLYFDAA SMLILLILTG KMLEQTAKNK ISEGLWKFFS LVPQKVRICA DQFPRGRYVS
IKQLSQGDAF LAEEGEILAA DGIVTRGSAV IDESSITGEA KPANVRPQDT VKSGTRIISG
KIQITAVKVG EDSILGRMLA IMENSLSEKT AQTQRFEDIL KFFVPSVIGF SIVTYFFWML
YGLTSYEAFN RGISVMVISC PCALGIAIPL ALVAGVSAAG KKGILVRDFE AFEKVNGLDT
IVFDKTGTLT TGKLKVLGMD TANNFPAQKA WQIVHAMEQE SDHYIAHTIS AFAMAMNLPP
LDLEDLTYHS NGISCQYQDK IYCFGSRDFV NKSNPADPSF ISFARQGAQV ISTVFLAQDD
TIVAAVHLGD AMKTGVKTLV ADLYKRGLTC YLISGDAERP TLAAGAFVQI PAENAHGGLL
PHEKAEFIKT LKQSGKKVAM VGDGVNDAPA MGQSDIAMAV HSGLNPGEGV AAITLMQETP
VQIIDFIGLA TRVNRKVKQN LIFALVYNII SIPVAAGGFL NPIIAATAML FSSLSVTCNT
LLLVKQESKN KPVS
//
