ID A7H9N7_ANADF Unreviewed; 944 AA.
AC A7H9N7;
DT 11-SEP-2007, integrated into UniProtKB/TrEMBL.
DT 11-SEP-2007, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:ABS25433.1};
GN OrderedLocusNames=Anae109_1225 {ECO:0000313|EMBL:ABS25433.1};
OS Anaeromyxobacter sp. (strain Fw109-5).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Anaeromyxobacteraceae; Anaeromyxobacter.
OX NCBI_TaxID=404589 {ECO:0000313|EMBL:ABS25433.1, ECO:0000313|Proteomes:UP000006382};
RN [1] {ECO:0000313|EMBL:ABS25433.1, ECO:0000313|Proteomes:UP000006382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fw109-5 {ECO:0000313|EMBL:ABS25433.1,
RC ECO:0000313|Proteomes:UP000006382};
RX PubMed=25614562; DOI=10.1128/genomeA.01449-14;
RA Hwang C., Copeland A., Lucas S., Lapidus A., Barry K., Glavina Del Rio T.,
RA Dalin E., Tice H., Pitluck S., Sims D., Brettin T., Bruce D.C.,
RA Detter J.C., Han C.S., Schmutz J., Larimer F.W., Land M.L., Hauser L.J.,
RA Kyrpides N., Lykidis A., Richardson P., Belieav A., Sanford R.A.,
RA Loeffler F.E., Fields M.W.;
RT "Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an anaerobic,
RT metal-reducing bacterium isolated from a contaminated subsurface
RT environment.";
RL Genome Announc. 3:0-0(2015).
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DR EMBL; CP000769; ABS25433.1; -; Genomic_DNA.
DR AlphaFoldDB; A7H9N7; -.
DR STRING; 404589.Anae109_1225; -.
DR KEGG; afw:Anae109_1225; -.
DR eggNOG; COG2217; Bacteria.
DR eggNOG; COG2608; Bacteria.
DR HOGENOM; CLU_001771_11_2_7; -.
DR Proteomes; UP000006382; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd00371; HMA; 1.
DR Gene3D; 3.30.70.100; -; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
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; 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; IPR001757; P_typ_ATPase.
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 PRINTS; PR00120; HATPASE.
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 SUPFAM; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000006382};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 168..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..258
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 421..442
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 454..476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 896..913
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 84..150
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 581..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 591..655
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 676..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 944 AA; 98118 MW; B2A135DAACFB8A96 CRC64;
MPVCDHCLLE FPAREAVEAE IGGEPRLFCC AGCRGVFELV HGEGLGAYYE TRRWDGPGAP
VKPDAFGPDL SAFREAVRHG EGGDEVEVYV DGIRCASCVW LNERLLSRTP GVTFARVNYA
THRARVRWDP ARADLETVLG RIRSAGYAPK PWSDSEQAAA RRAEEKDLLV RLGTAGFLAS
QLMIYQAALY AGYFQGIDAG TRRLMEWISL GLTLPVFFYA GASFLRATAS GLRHLRFNMD
SLVVFGSGAA LAYSVYQMSR GGEVYFDTAA MIPTLVLVGR FVEAGAKGRA SEAVARLARL
APREARRLER RGDGREEPRS VPVAELRAGD RVSIVPGERV PVDGSVLDGT SDVDESLVTG
ESRPVAKGAG ASVIGGTVNG TGSLVVEVTR TGKDTVLAGI VRAVEEAQTA KPRIQAVADR
VVGVFVPAML VLAAATLAYW LARGAPLDRA IMTGISVVVI ACPCALGLAT PIAVIVSTGL
ATQRGLLVKG GDVVERAGRA TDVLLDKTGT VTRGRPVLRE VAVLDAALAS EDALALAAAV
ESRSEHHVGR AIAEAARALP EAAAVEVEGF RAVPGRGVVA TVRATPTPTP TATPTATPTP
TPTPTPTPTP TPTPTPTSTS TPTPTPTPTP TATPTPTPTP TPTPTPTPTP TPTPTPTSTS
TSTSTPTPTP TPTSTPTSTP TSTSTSTSTS TSTATSTSTP TSTSTSTSTA TSTSTSRAVL
IGNRALLADH GIALPPDADA AGRAIEARGE TVAFLAIDGA PAALFAIADV VRDEAPEAIA
RLRALGLRVA IVSGDTRVTT EAVAEGLGVE SVAEASPVEK RAVVARLQAE GRRVLFAGDG
INDAPALTQA DVGAAMGRGT DVTMESADAV LVRDDLRLVP DLVRLSRRTY AVIRQNVFWA
FFYNVVAIPL AMAGVLHPIV AAGAMAASSL FVVLNSVRLR GALG
//
