KDPA_MYCPA
ID KDPA_MYCPA Reviewed; 556 AA.
AC Q741T7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Potassium-transporting ATPase potassium-binding subunit {ECO:0000255|HAMAP-Rule:MF_00275};
DE AltName: Full=ATP phosphohydrolase [potassium-transporting] A chain {ECO:0000255|HAMAP-Rule:MF_00275};
DE AltName: Full=Potassium-binding and translocating subunit A {ECO:0000255|HAMAP-Rule:MF_00275};
DE AltName: Full=Potassium-translocating ATPase A chain {ECO:0000255|HAMAP-Rule:MF_00275};
GN Name=kdpA {ECO:0000255|HAMAP-Rule:MF_00275}; OrderedLocusNames=MAP_1000c;
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10;
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
CC -!- FUNCTION: Part of the high-affinity ATP-driven potassium transport (or
CC Kdp) system, which catalyzes the hydrolysis of ATP coupled with the
CC electrogenic transport of potassium into the cytoplasm. This subunit
CC binds the extracellular potassium ions and delivers the ions to the
CC membrane domain of KdpB through an intramembrane tunnel.
CC {ECO:0000255|HAMAP-Rule:MF_00275}.
CC -!- SUBUNIT: The system is composed of three essential subunits: KdpA, KdpB
CC and KdpC. {ECO:0000255|HAMAP-Rule:MF_00275}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00275};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00275}.
CC -!- SIMILARITY: Belongs to the KdpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00275}.
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DR EMBL; AE016958; AAS03317.1; -; Genomic_DNA.
DR RefSeq; WP_003877548.1; NC_002944.2.
DR AlphaFoldDB; Q741T7; -.
DR SMR; Q741T7; -.
DR STRING; 262316.MAP_1000c; -.
DR PRIDE; Q741T7; -.
DR EnsemblBacteria; AAS03317; AAS03317; MAP_1000c.
DR KEGG; mpa:MAP_1000c; -.
DR PATRIC; fig|262316.17.peg.1045; -.
DR eggNOG; COG2060; Bacteria.
DR HOGENOM; CLU_018614_3_0_11; -.
DR OMA; RQGWAIL; -.
DR Proteomes; UP000000580; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008556; F:P-type potassium transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00275; KdpA; 1.
DR InterPro; IPR004623; KdpA.
DR PANTHER; PTHR30607; PTHR30607; 1.
DR Pfam; PF03814; KdpA; 1.
DR PIRSF; PIRSF001294; K_ATPaseA; 1.
DR TIGRFAMs; TIGR00680; kdpA; 1.
PE 3: Inferred from homology;
KW Cell membrane; Ion transport; Membrane; Potassium; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..556
FT /note="Potassium-transporting ATPase potassium-binding
FT subunit"
FT /id="PRO_0000166508"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 65..85
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 249..269
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 483..503
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 526..546
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ SEQUENCE 556 AA; 58396 MW; 39995D037757D574 CRC64;
MSSTTAGLIF LAVLVAALVA VHVPLGDYMF RVYTTDRDLA TERTIYRLIG VDARSEQTWG
AYARGVLAFS SVSIIFLFVL QLVQGKLPLH LHDPATKMTP SLAWNTAVSF VTNTNWQAYS
GETTQGHLVQ MAGLAVQNFV SAAVGMAVAV ALVRGFARRR TGELGNFWVD LVRGTLRILL
PISIVGAVLL VAGGAIQNFH LHDQVVTTLG GTAQTIPGGP VASQEVIKEL ATNGGGFYNA
NSAHPFENPT AWTNWLEVFL ILVIGFSLPR TFGRMVGNPK QGYAIASVMA SLYLLSTGFM
LWFQLQHHGT VPSAVGAAME GVEQRFGVPD SGVFAAATTL TSTGAVDSAH DSLTSLGGMI
TMFNMQLGEV APGGTGSGLY GMLVLAVITV FVAGLMVGRT PEYLGKKINP REIKLAASYF
LVTPLIVLTG TAIAMALPGE RAGMANSGPH GLSEVLYAFT SAANNNGSAF AGLSANTEWY
NTALGLAMAF GRFLPIVLVL ALAGSLARQG STPDSAGTLP THRPQFVGMV AGVTLIVVAL
TFLPMLALGP LAEGIH