ID A0A0F7H9R4_SERFO Unreviewed; 778 AA.
AC A0A0F7H9R4;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Zinc ABC transporter ATPase {ECO:0000313|EMBL:AKG69321.1};
DE EC=3.6.3.3 {ECO:0000313|EMBL:AKG69321.1};
DE EC=3.6.3.5 {ECO:0000313|EMBL:AKG69321.1};
GN Name=zntA {ECO:0000313|EMBL:AKG69321.1};
GN ORFNames=WN53_09485 {ECO:0000313|EMBL:AKG69321.1};
OS Serratia fonticola.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=47917 {ECO:0000313|EMBL:AKG69321.1, ECO:0000313|Proteomes:UP000034699};
RN [1] {ECO:0000313|EMBL:AKG69321.1, ECO:0000313|Proteomes:UP000034699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4576 {ECO:0000313|EMBL:AKG69321.1,
RC ECO:0000313|Proteomes:UP000034699};
RA Chan K.-G., Ee R.;
RT "Complete Genome Sequencing of Serratia Fonticola DSM-4576.";
RL Submitted (APR-2015) 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; CP011254; AKG69321.1; -; Genomic_DNA.
DR RefSeq; WP_024484643.1; NZ_CP011254.1.
DR AlphaFoldDB; A0A0F7H9R4; -.
DR STRING; 47917.AV650_01515; -.
DR GeneID; 30320392; -.
DR KEGG; sfw:WN53_09485; -.
DR PATRIC; fig|47917.8.peg.1972; -.
DR Proteomes; UP000034699; 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 GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd00371; HMA; 1.
DR CDD; cd07546; P-type_ATPase_Pb_Zn_Cd2-like; 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 InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
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; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00941; CDATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 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; PS01229; COF_2; 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 Hydrolase {ECO:0000313|EMBL:AKG69321.1};
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:UP000034699};
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 169..188
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 195..216
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 228..257
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..445
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 727..747
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 86..150
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 1..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 778 AA; 81966 MW; 3F348D1CED47EBFF CRC64;
MQTHKPHNHQ EHQHQEHNHD HGCGCSHDHA KTQHGCSTEK TPVGATAAHD HQAAHEHGTS
CCSSDGPDDP DEESDRLAAV PPSGSQRFSW KVTGMDCPSC AKKIENAVTS IPGVDSARVL
FATEKLVVDA QSDVSMRIQD AVKQAGFTLL GTTPAAQGDE PKTSRFGEYG PLILLSALMV
LSWVLDFFNP RLGEIAFIAT TLVGLVPIAS KALRLIRSGT PFAIETLMSV AAIGALFIGA
TAEAAMVLLL FMVGELLESY AANRARRGVK ALMELVPEDA LLIQGSVRKR VPVASLRPGD
VIEIAPGGRL PADAELLNPF ASFDESALTG ESVPVERQQG QKVAAGSLSV DQAAQMKVTS
EPGKNAIDRI LQLIEEAEER RAPIERFLDR FSRYYTPAIM LLAVAVILVP PLLFAEAWEM
WIYRGLTLLL IGCPCALVIS TPAAITSGLA AATRRGALIK GGAALEQLGQ VQTIAFDKTG
TLTEGKPTVT DVLPAAGLSE QQLLAIAAAV EAGSHHPLAQ AIVNRAAENG AALPLAEGRR
ALAGIGVEGK VDGKTILIST PGKLTESQLS SEWRSQVETL ETAGKTAVVV LEDGQPIGLL
ALRDTLRSDA KQAIAELAQL GVRGVMLTGD NPRAAAAIAN ELGIDYRAGL MPEDKVNAVT
ELSKLQPTAM IGDGINDAPA MKAASIGIAM GSGTDVALET ADAALTHNRL TGVAEMIRIS
RATHANIRQN ITIALGLKAI FLVTTLLGMT GLWLAVLADS GATALVTANA LRLLKKRQ
//
