ID M4RKH4_9ALTE Unreviewed; 932 AA.
AC M4RKH4;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:AGH44061.1};
GN ORFNames=C427_1952 {ECO:0000313|EMBL:AGH44061.1};
OS Paraglaciecola psychrophila 170.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1129794 {ECO:0000313|EMBL:AGH44061.1, ECO:0000313|Proteomes:UP000011864};
RN [1] {ECO:0000313|EMBL:AGH44061.1, ECO:0000313|Proteomes:UP000011864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=170 {ECO:0000313|EMBL:AGH44061.1,
RC ECO:0000313|Proteomes:UP000011864};
RX PubMed=23640379;
RA Yin J., Chen J., Liu G., Yu Y., Song L., Wang X., Qu X.;
RT "Complete Genome Sequence of Glaciecola psychrophila Strain 170T.";
RL Genome Announc. 1:E00199-13(2013).
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; CP003837; AGH44061.1; -; Genomic_DNA.
DR AlphaFoldDB; M4RKH4; -.
DR STRING; 1129794.C427_1952; -.
DR KEGG; gps:C427_1952; -.
DR PATRIC; fig|1129794.4.peg.1933; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_6; -.
DR Proteomes; UP000011864; 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:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00371; HMA; 2.
DR CDD; cd01108; HTH_CueR; 1.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 1.10.1660.10; -; 1.
DR Gene3D; 3.30.70.100; -; 2.
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; IPR011789; CueR.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006122; HMA_Cu_ion-bd.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR000551; MerR-type_HTH_dom.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR InterPro; IPR015358; Tscrpt_reg_MerR_DNA-bd.
DR NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR NCBIfam; TIGR00003; copper ion binding protein; 1.
DR NCBIfam; TIGR02044; CueR; 1.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF00376; MerR; 1.
DR Pfam; PF09278; MerR-DNA-bind; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00941; CDATPASE.
DR PRINTS; PR00040; HTHMERR.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00422; HTH_MERR; 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; 2.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01229; COF_2; 1.
DR PROSITE; PS01047; HMA_1; 2.
DR PROSITE; PS50846; HMA_2; 2.
DR PROSITE; PS50937; HTH_MERR_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Copper {ECO:0000256|ARBA:ARBA00023008};
KW Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW Ion transport {ECO:0000256|ARBA:ARBA00022796};
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:UP000011864};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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}; Transport {ECO:0000256|ARBA:ARBA00022796}.
FT TRANSMEM 164..186
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 192..210
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 222..243
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 255..273
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 410..431
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 437..460
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 747..763
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 769..789
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 3..66
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 68..138
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 802..871
FT /note="HTH merR-type"
FT /evidence="ECO:0000259|PROSITE:PS50937"
FT COILED 883..910
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 932 AA; 99938 MW; 144C6E92A93C5816 CRC64;
MQSSMQLAVQ GMTCSSCAGR IEKALLKVEN VEQASVNLAT ETVTVEGNPS VNELVKAITG
AGYQVSTETR QYQLTGMTCA SCAGRVEKAL LNVAGVITAN VNLATEQVNI TLLSKMSEAS
LNESMLGEAV KNAGYQLVSQ QSLAEQAETH NQTMAFFRSD NWPVIGASLL TLPLVLPMLG
MLFGINWVMP SLWQWLLATP VQFYFGARFY RAGFNALKAG TSNMDLLVAI GTSAAYGLSL
YLWYSFDGEH GAPHLYFESS AAVLTLVLLG KLLEQRAKRH TTDALRALES LKPTTANVWR
NENWQSVAAI ELQRDEKVKV LPGERIPVDG KVIKGDSHVD EALISGESMP LLKSIGDKVT
GGSINLDGVL ELTATAVGAE STLAKIIHMV EQAQGAKAPV QALVDKISSV FVPLVLVIAL
LTLLGWGMIS GDWTQGILHA VAVLVIACPC ALGLATPAAI MAGTGTAARH GILVKDARAL
EQAKQTDMVV FDKTGTLTEG KPELIQLTAF QIDEPALLTL AYGLQQNSEH PLAKAVVKRA
QQDATKLPDI KHFKVIAGKG VQGEENGKQL LLGSSRWMQE LGLTLPLQQI TTQGATVSWL
ASKQGENIEL LGLLCFADKI KEQAKHAVDA LKHRGIKVAM LTGDSAASAQ QVASELGLDD
YQAEVLPQDK AAAIASYQQQ GYQVAMVGDG INDAPALAQA DLGIAMATGT EVAISAAAIT
LMRGDPALVS AAISLASATY RNIQQNLFWA FAFNSVGIPL AALGYLNPII AGGAMAVSSV
LVVTNALRLQ RKSFKRGNMN TLLTIGNAAK ASGLTAKMIR HYEESSLLQR PPRTEAGYRL
YNSEQLNQLK FIRQARNLGF SLHEIKSLLS LWQDPQRESR AVKQMAEQHL AEIETKIAEL
QHMQQVLTEL ATSCRGDSSP DCSILQQLAK GE
//
