ID A0A098QZ35_9SPIO Unreviewed; 779 AA.
AC A0A098QZ35;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=HMA domain-containing protein {ECO:0000259|PROSITE:PS50846};
GN ORFNames=DC28_10930 {ECO:0000313|EMBL:KGE71747.1};
OS Spirochaeta lutea.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Spirochaeta.
OX NCBI_TaxID=1480694 {ECO:0000313|EMBL:KGE71747.1, ECO:0000313|Proteomes:UP000029692};
RN [1] {ECO:0000313|EMBL:KGE71747.1, ECO:0000313|Proteomes:UP000029692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC230 {ECO:0000313|EMBL:KGE71747.1,
RC ECO:0000313|Proteomes:UP000029692};
RA Shivani Y., Subhash Y., Tushar L., Sasikala C., Ramana C.V.;
RT "De novo Genome Sequence of Spirocheata sp.";
RL Submitted (MAY-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGE71747.1}.
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; JNUP01000065; KGE71747.1; -; Genomic_DNA.
DR RefSeq; WP_037548223.1; NZ_JNUP01000065.1.
DR AlphaFoldDB; A0A098QZ35; -.
DR STRING; 1480694.DC28_10930; -.
DR eggNOG; COG2217; Bacteria.
DR OrthoDB; 9760364at2; -.
DR Proteomes; UP000029692; Unassembled WGS sequence.
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; IPR017969; Heavy-metal-associated_CS.
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; 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; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00941; CDATPASE.
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; PS01047; HMA_1; 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|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000029692};
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 139..165
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 185..208
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 394..415
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 421..446
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 727..747
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 753..774
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 3..65
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 63..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..108
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 779 AA; 82521 MW; A591F7981A835636 CRC64;
METIKKYRIE GIDCANCAAD IERALQRHPG LEQARINLAT QTLGINPGYL DTARSVIASM
EPQVRVSDRR EPSRSPAELG KTAGMSEGTA NPSRGGEQVR NAGTSEGAGG PSSAAGRGLL
GVVSGLRTSL SRFFEDRELL RLAAGGLFFL GGIILGSVTS GAVSMALRGS LLGLFGLQAG
PGLGWLQGFT GIQALFTTAF IITGWPVVWS ALRNLVRGAV FDETLLMTIA TLGAAAIGEL
AESAGVMIFY GVGEWLQDRA VNRSRQSISA LVDLRPDTLR LVVPGGETRT IPASEAEPDQ
VIEHWPGERI GVDGILESAQ GSFDTSALTG ESVPRTIRRG EEVAAGFLVT DSPVRLRVTR
RVEDSAVSRI LNLVEDATDK KAKTERFIAR FARIYTPLVV AAALGVALVP PLAFGGDLNQ
WVYRALTILV ISCPCALVIS IPLGYFAGLG AASRRGVLVK GAEYLDRLAS LSGLAFDKTG
TLTKGVFEVR RVRVSEGFSE DGVIRMAAEA EAMSSHPIAR AILSYAEGGG ISPGSREEQE
RTEHRGMGIT LKEQDRSIAV GNGRLMEDLG IQVPQDGLGG TVVYVALDGR YAGVLEIDDE
VKPGTWDHIQ DLKRAGVSRM TMVTGDREEP AVRMARDLGI TGVRHSLLPE DKVSVLEGFM
QEDRGTSGFI GDGINDAPVL ARADVGIAMG GLGSDAAIEA ADVVLMSDSL GALGDGIRIG
RQTRRIILQN IIFALGFKAI IMIFGILGEA TMWQAVIADV GVALVAVLNS IRILPGTRS
//