KDPA_ECOLI
ID KDPA_ECOLI Reviewed; 557 AA.
AC P03959;
DT 23-OCT-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 168.
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};
GN OrderedLocusNames=b0698, JW0686;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6146979; DOI=10.1073/pnas.81.15.4746;
RA Hesse J.E., Wieczorek L., Altendorf K., Reicin A.S., Dorus E., Epstein W.;
RT "Sequence homology between two membrane transport ATPases, the Kdp-ATPase
RT of Escherichia coli and the Ca2+-ATPase of sarcoplasmic reticulum.";
RL Proc. Natl. Acad. Sci. U.S.A. 81:4746-4750(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION IN POTASSIUM TRANSPORT, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=2849541; DOI=10.1111/j.1432-1033.1988.tb14438.x;
RA Siebers A., Altendorf K.;
RT "The K+-translocating Kdp-ATPase from Escherichia coli. Purification,
RT enzymatic properties and production of complex- and subunit-specific
RT antisera.";
RL Eur. J. Biochem. 178:131-140(1988).
RN [6]
RP INDUCTION.
RC STRAIN=K12;
RX PubMed=1532387; DOI=10.1128/jb.174.7.2145-2151.1992;
RA Polarek J.W., Williams G., Epstein W.;
RT "The products of the kdpDE operon are required for expression of the Kdp
RT ATPase of Escherichia coli.";
RL J. Bacteriol. 174:2145-2151(1992).
RN [7]
RP FUNCTION IN POTASSIUM TRANSPORT.
RC STRAIN=K12;
RX PubMed=8499455; DOI=10.1016/0005-2728(93)90216-3;
RA Kollmann R., Altendorf K.;
RT "ATP-driven potassium transport in right-side-out membrane vesicles via the
RT Kdp system of Escherichia coli.";
RL Biochim. Biophys. Acta 1143:62-66(1993).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, AND POTASSIUM-BINDING SITES.
RX PubMed=7896809; DOI=10.1074/jbc.270.12.6678;
RA Buurman E.T., Kim K.T., Epstein W.;
RT "Genetic evidence for two sequentially occupied K+ binding sites in the Kdp
RT transport ATPase.";
RL J. Biol. Chem. 270:6678-6685(1995).
RN [9]
RP SUBUNIT.
RC STRAIN=K12;
RX PubMed=9858692; DOI=10.1016/s0005-2736(98)00179-5;
RA Gassel M., Siebers A., Epstein W., Altendorf K.;
RT "Assembly of the Kdp complex, the multi-subunit K+-transport ATPase of
RT Escherichia coli.";
RL Biochim. Biophys. Acta 1415:77-84(1998).
RN [10]
RP SUBUNIT.
RC STRAIN=K12;
RX PubMed=10608856; DOI=10.1074/jbc.274.53.37901;
RA Gassel M., Mollenkamp T., Puppe W., Altendorf K.;
RT "The KdpF subunit is part of the K(+)-translocating Kdp complex of
RT Escherichia coli and is responsible for stabilization of the complex in
RT vitro.";
RL J. Biol. Chem. 274:37901-37907(1999).
RN [11]
RP MUTAGENESIS OF GLY-232.
RX PubMed=12218037; DOI=10.1128/jb.184.19.5491-5494.2002;
RA van der Laan M., Gassel M., Altendorf K.;
RT "Characterization of amino acid substitutions in KdpA, the K+-binding and
RT -translocating subunit of the KdpFABC complex of Escherichia coli.";
RL J. Bacteriol. 184:5491-5494(2002).
RN [12]
RP SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [13]
RP SUBUNIT.
RX PubMed=18298081; DOI=10.1021/bi702038e;
RA Heitkamp T., Kalinowski R., Boettcher B., Boersch M., Altendorf K.,
RA Greie J.C.;
RT "K+-translocating KdpFABC P-type ATPase from Escherichia coli acts as a
RT functional and structural dimer.";
RL Biochemistry 47:3564-3575(2008).
RN [14]
RP FUNCTION.
RX PubMed=23930894; DOI=10.1021/bi400729e;
RA Damnjanovic B., Weber A., Potschies M., Greie J.C., Apell H.J.;
RT "Mechanistic analysis of the pump cycle of the KdpFABC P-type ATPase.";
RL Biochemistry 52:5563-5576(2013).
RN [15] {ECO:0007744|PDB:5MRW}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF MUTANT ARG-116 IN COMPLEX WITH
RP KDPB; KDPC AND KDPF, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, AND DOMAIN.
RX PubMed=28636601; DOI=10.1038/nature22970;
RA Huang C.S., Pedersen B.P., Stokes D.L.;
RT "Crystal structure of the potassium-importing KdpFABC membrane complex.";
RL Nature 546:681-685(2017).
RN [16] {ECO:0007744|PDB:6HRA, ECO:0007744|PDB:6HRB}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.70 ANGSTROMS) OF KDPFABC COMPLEX IN E1
RP AND E2 STATE, FUNCTION, REACTION MECHANISM, SUBUNIT, SUBCELLULAR LOCATION,
RP AND DOMAIN.
RX PubMed=30478378; DOI=10.1038/s41467-018-07319-2;
RA Stock C., Hielkema L., Tascon I., Wunnicke D., Oostergetel G.T.,
RA Azkargorta M., Paulino C., Haenelt I.;
RT "Cryo-EM structures of KdpFABC suggest a K+ transport mechanism via two
RT inter-subunit half-channels.";
RL Nat. Commun. 9:4971-4971(2018).
RN [17] {ECO:0007744|PDB:7BGY, ECO:0007744|PDB:7BH1, ECO:0007744|PDB:7BH2, ECO:0007744|PDB:7LC3, ECO:0007744|PDB:7LC6}
RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) OF KDPFABC COMPLEX IN
RP MAJOR ENZYMATIC STATES, FUNCTION, REACTION MECHANISM, AND DOMAIN.
RX PubMed=34272288; DOI=10.1073/pnas.2105195118;
RA Sweet M.E., Larsen C., Zhang X., Schlame M., Pedersen B.P., Stokes D.L.;
RT "Structural basis for potassium transport in prokaryotes by KdpFABC.";
RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021).
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
CC (PubMed:23930894, PubMed:2849541, PubMed:8499455). This subunit binds
CC the periplasmic potassium ions and delivers the ions to the membrane
CC domain of KdpB through an intramembrane tunnel (PubMed:7896809,
CC PubMed:30478378, PubMed:34272288). {ECO:0000269|PubMed:23930894,
CC ECO:0000269|PubMed:2849541, ECO:0000269|PubMed:30478378,
CC ECO:0000269|PubMed:34272288, ECO:0000269|PubMed:7896809,
CC ECO:0000269|PubMed:8499455}.
CC -!- SUBUNIT: The system is composed of three essential subunits: KdpA, KdpB
CC and KdpC (PubMed:2849541, PubMed:9858692, PubMed:28636601,
CC PubMed:30478378). The complex also contains KdpF, a small non-essential
CC subunit (PubMed:10608856, PubMed:28636601, PubMed:30478378). The
CC KdpFABC complex exists as a dimer above concentrations of 30-50 nM,
CC whereas the complex exists as a functional monomer at lower
CC concentrations (PubMed:18298081). {ECO:0000269|PubMed:10608856,
CC ECO:0000269|PubMed:18298081, ECO:0000269|PubMed:2849541,
CC ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378,
CC ECO:0000269|PubMed:9858692}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00275, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:2849541,
CC ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378,
CC ECO:0000269|PubMed:7896809}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_00275, ECO:0000269|PubMed:28636601,
CC ECO:0000269|PubMed:30478378, ECO:0000269|PubMed:7896809}.
CC -!- INDUCTION: Transcriptionally regulated by the KdpD/KdpE two-component
CC regulatory system. {ECO:0000269|PubMed:1532387}.
CC -!- DOMAIN: A protein-embedded tunnel connects the potassium ion in KdpA to
CC a water molecule at the canonical cation site in the transmembrane
CC domain of KdpB (PubMed:28636601, PubMed:30478378, PubMed:34272288). The
CC structures suggest a translocation pathway for potassium via two inter-
CC subunit half-channels along KdpA and KdpB, integrating KdpB directly in
CC the transport process (PubMed:30478378). The periplasmic potassium ion
CC probably enters the selectivity filter of KdpA, travels through the
CC water-filled tunnel to reach KdpB, and is released to the cytoplasm by
CC KdpB (PubMed:34272288). KdpB undergoes conformational changes, whereas
CC KdpA, KdpC and KdpF remain static (PubMed:34272288).
CC {ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378,
CC ECO:0000269|PubMed:34272288}.
CC -!- MISCELLANEOUS: Has two separate and distinct potassium-binding sites.
CC One site is formed by three periplasmic loops and is inferred to be the
CC site of initial binding. The other site is cytoplasmic.
CC {ECO:0000269|PubMed:7896809}.
CC -!- SIMILARITY: Belongs to the KdpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00275}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; K02670; AAB96335.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73792.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35356.1; -; Genomic_DNA.
DR PIR; A01071; PWECAK.
DR RefSeq; NP_415226.1; NC_000913.3.
DR RefSeq; WP_000741129.1; NZ_LN832404.1.
DR PDB; 5MRW; X-ray; 2.90 A; A/E/I=1-557.
DR PDB; 6HRA; EM; 3.70 A; A=1-557.
DR PDB; 6HRB; EM; 4.00 A; A=1-557.
DR PDB; 7BGY; EM; 2.90 A; A=1-557.
DR PDB; 7BH1; EM; 3.38 A; A=1-557.
DR PDB; 7BH2; EM; 3.00 A; A=1-557.
DR PDB; 7LC3; EM; 3.23 A; A=1-557.
DR PDB; 7LC6; EM; 3.70 A; A=1-557.
DR PDB; 7NNL; EM; 3.10 A; A=1-557.
DR PDB; 7NNP; EM; 3.20 A; A=1-557.
DR PDBsum; 5MRW; -.
DR PDBsum; 6HRA; -.
DR PDBsum; 6HRB; -.
DR PDBsum; 7BGY; -.
DR PDBsum; 7BH1; -.
DR PDBsum; 7BH2; -.
DR PDBsum; 7LC3; -.
DR PDBsum; 7LC6; -.
DR PDBsum; 7NNL; -.
DR PDBsum; 7NNP; -.
DR AlphaFoldDB; P03959; -.
DR SMR; P03959; -.
DR BioGRID; 4259932; 35.
DR ComplexPortal; CPX-3564; KdpFABC potassium import complex.
DR IntAct; P03959; 3.
DR STRING; 511145.b0698; -.
DR TCDB; 3.A.3.7.1; the p-type atpase (p-atpase) superfamily.
DR PaxDb; P03959; -.
DR PRIDE; P03959; -.
DR DNASU; 946045; -.
DR EnsemblBacteria; AAC73792; AAC73792; b0698.
DR EnsemblBacteria; BAA35356; BAA35356; BAA35356.
DR GeneID; 946045; -.
DR KEGG; ecj:JW0686; -.
DR KEGG; eco:b0698; -.
DR PATRIC; fig|1411691.4.peg.1577; -.
DR EchoBASE; EB0508; -.
DR eggNOG; COG2060; Bacteria.
DR HOGENOM; CLU_018614_3_0_6; -.
DR InParanoid; P03959; -.
DR OMA; RQGWAIL; -.
DR PhylomeDB; P03959; -.
DR BioCyc; EcoCyc:EG10513-MON; -.
DR BioCyc; MetaCyc:EG10513-MON; -.
DR BRENDA; 7.2.2.6; 2026.
DR PRO; PR:P03959; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0031004; C:potassium ion-transporting ATPase complex; IDA:EcoCyc.
DR GO; GO:1903103; C:potassium:proton antiporter complex; IPI:ComplexPortal.
DR GO; GO:0008556; F:P-type potassium transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0030955; F:potassium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0098655; P:cation transmembrane transport; IDA:EcoCyc.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:EcoCyc.
DR GO; GO:0006813; P:potassium ion transport; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW Potassium; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..557
FT /note="Potassium-transporting ATPase potassium-binding
FT subunit"
FT /id="PRO_0000166494"
FT TOPO_DOM 1..2
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0000305|PubMed:7896809"
FT TRANSMEM 3..27
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0007744|PDB:5MRW"
FT TOPO_DOM 28..61
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0000305|PubMed:7896809"
FT TRANSMEM 62..84
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0007744|PDB:5MRW"
FT TOPO_DOM 85..125
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0000305|PubMed:7896809"
FT TRANSMEM 126..149
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0007744|PDB:5MRW"
FT TOPO_DOM 150..165
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0000305|PubMed:7896809"
FT TRANSMEM 166..192
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0007744|PDB:5MRW"
FT TOPO_DOM 193..249
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0000305|PubMed:7896809"
FT TRANSMEM 250..269
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0007744|PDB:5MRW"
FT TOPO_DOM 270..279
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0000305|PubMed:7896809"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0007744|PDB:5MRW"
FT TOPO_DOM 301..356
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0000305|PubMed:7896809"
FT TRANSMEM 357..368
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0007744|PDB:5MRW"
FT TOPO_DOM 369..414
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0000305|PubMed:7896809"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0007744|PDB:5MRW"
FT TOPO_DOM 436..479
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0000305|PubMed:7896809"
FT TRANSMEM 480..501
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0007744|PDB:5MRW"
FT TOPO_DOM 502..524
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0000305|PubMed:7896809"
FT TRANSMEM 525..552
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0007744|PDB:5MRW"
FT TOPO_DOM 553..557
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:28636601,
FT ECO:0000305|PubMed:7896809"
FT MUTAGEN 232
FT /note="G->A,S: Decrease in K(+) affinity and loss of cation
FT selectivity."
FT /evidence="ECO:0000269|PubMed:12218037"
FT HELIX 2..31
FT /evidence="ECO:0007829|PDB:5MRW"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:7LC3"
FT HELIX 41..50
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 59..82
FT /evidence="ECO:0007829|PDB:5MRW"
FT TURN 83..86
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 126..130
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 133..156
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 166..176
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 178..192
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 219..228
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 235..238
FT /evidence="ECO:0007829|PDB:5MRW"
FT TURN 239..241
FT /evidence="ECO:0007829|PDB:5MRW"
FT TURN 243..245
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 249..273
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 278..304
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 307..311
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:7BH2"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 329..341
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 356..367
FT /evidence="ECO:0007829|PDB:5MRW"
FT TURN 375..377
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 378..398
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 411..435
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 439..442
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 450..464
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 479..508
FT /evidence="ECO:0007829|PDB:5MRW"
FT STRAND 517..519
FT /evidence="ECO:0007829|PDB:7LC3"
FT HELIX 524..548
FT /evidence="ECO:0007829|PDB:5MRW"
FT HELIX 551..556
FT /evidence="ECO:0007829|PDB:5MRW"
SQ SEQUENCE 557 AA; 59189 MW; 88C397FC3D3DC17E CRC64;
MAAQGFLLIA TFLLVLMVLA RPLGSGLARL INDIPLPGTT GVERVLFRAL GVSDREMNWK
QYLCAILGLN MLGLAVLFFM LLGQHYLPLN PQQLPGLSWD LALNTAVSFV TNTNWQSYSG
ETTLSYFSQM AGLTVQNFLS AASGIAVIFA LIRAFTRQSM STLGNAWVDL LRITLWVLVP
VALLIALFFI QQGALQNFLP YQAVNTVEGA QQLLPMGPVA SQEAIKMLGT NGGGFFNANS
SHPFENPTAL TNFVQMLAIF LIPTALCFAF GEVMGDRRQG RMLLWAMSVI FVICVGVVMW
AEVQGNPHLL ALGTDSSINM EGKESRFGVL VSSLFAVVTT AASCGAVIAM HDSFTALGGM
VPMWLMQIGE VVFGGVGSGL YGMMLFVLLA VFIAGLMIGR TPEYLGKKID VREMKLTALA
ILVTPTLVLM GAALAMMTDA GRSAMLNPGP HGFSEVLYAV SSAANNNGSA FAGLSANSPF
WNCLLAFCMF VGRFGVIIPV MAIAGSLVSK KSQAASSGTL PTHGPLFVGL LIGTVLLVGA
LTFIPALALG PVAEYLS
