KDPA_CUTAK
ID KDPA_CUTAK Reviewed; 556 AA.
AC Q6ABJ2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 115.
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=PPA0115;
OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS acnes).
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Cutibacterium.
OX NCBI_TaxID=267747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202;
RX PubMed=15286373; DOI=10.1126/science.1100330;
RA Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT "The complete genome sequence of Propionibacterium acnes, a commensal of
RT human skin.";
RL Science 305:671-673(2004).
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; AE017283; AAT81875.1; -; Genomic_DNA.
DR RefSeq; WP_002515780.1; NZ_CP025935.1.
DR AlphaFoldDB; Q6ABJ2; -.
DR SMR; Q6ABJ2; -.
DR STRING; 267747.PPA0115; -.
DR EnsemblBacteria; AAT81875; AAT81875; PPA0115.
DR KEGG; pac:PPA0115; -.
DR PATRIC; fig|267747.3.peg.119; -.
DR eggNOG; COG2060; Bacteria.
DR HOGENOM; CLU_018614_3_0_11; -.
DR OMA; RQGWAIL; -.
DR Proteomes; UP000000603; 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 Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..556
FT /note="Potassium-transporting ATPase potassium-binding
FT subunit"
FT /id="PRO_0000166512"
FT TRANSMEM 1..21
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 374..394
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 416..436
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
FT TRANSMEM 529..549
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00275"
SQ SEQUENCE 556 AA; 58602 MW; 726F158F3B17D0B0 CRC64;
MTWICFLAGL ALLAIALGIA QHHLGTYMAR VFTSDKDTRV ETWCYRVMGV NPRAGQTWKS
YARAVLAFSF CGVVFLYALQ RLQPWLPWSL GKGSVNPAVS FNTAISFVTN TNWQAYSPEA
TLGHFVQLAG LCVQNFVSAA TGIAIAVALI RGFVGHGEHT IGNFWVDLTR CTLRILMPIA
AVAAFLLIAG GAVQNFTGFL HVTGVAGGNQ VIPGGPVASQ EAIKELGTNG GGFFNGNSSH
PFENPQPWTN MLEIFLILLI PFSLPRTFGK MVEDVRQGRA ILAAMVVLFT VNLCAMAAAE
FSGHGTAARL AGAPMEGKEQ RFGLAQSVLF ANSTTMTSTG AVDSMHDSFT AIGGMFTLLN
MMLGEISPGG VGSGLYGMLV IAVIAVFIAG LLVGRTPEYL GKKIGPREMK LSDLYILVMP
TLVLCGVALS LAVPGLRSSV NTSIANPGEH GLSELVYAFT SAANNNGSAF AGLDASTNWL
CAALGAAMLL GRFVPIILIL ALSGALVERE PVPVTAGTLP THNALFTTLI VFTAILVTAL
VFFPVLTLGP LAEGLI