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Database: UniProt
Entry: A0A2K1KKU2_PHYPA
LinkDB: A0A2K1KKU2_PHYPA
Original site: A0A2K1KKU2_PHYPA 
ID   A0A2K1KKU2_PHYPA        Unreviewed;       729 AA.
AC   A0A2K1KKU2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN   ORFNames=PHYPA_008073 {ECO:0000313|EMBL:PNR54396.1};
OS   Physcomitrium patens (Spreading-leaved earth moss) (Physcomitrella patens).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Bryophyta;
OC   Bryophytina; Bryopsida; Funariidae; Funariales; Funariaceae; Physcomitrium.
OX   NCBI_TaxID=3218 {ECO:0000313|EMBL:PNR54396.1};
RN   [1] {ECO:0000313|EMBL:PNR54396.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c5_23480V3.1,
RC   ECO:0000313|Proteomes:UP000006727};
RX   PubMed=18079367; DOI=10.1126/science.1150646;
RA   Rensing S.A., Lang D., Zimmer A.D., Terry A., Salamov A., Shapiro H.,
RA   Nishiyama T., Perroud P.-F., Lindquist E.A., Kamisugi Y., Tanahashi T.,
RA   Sakakibara K., Fujita T., Oishi K., Shin-I T., Kuroki Y., Toyoda A.,
RA   Suzuki Y., Hashimoto S.-I., Yamaguchi K., Sugano S., Kohara Y.,
RA   Fujiyama A., Anterola A., Aoki S., Ashton N., Barbazuk W.B., Barker E.,
RA   Bennetzen J.L., Blankenship R., Cho S.H., Dutcher S.K., Estelle M.,
RA   Fawcett J.A., Gundlach H., Hanada K., Heyl A., Hicks K.A., Hughes J.,
RA   Lohr M., Mayer K., Melkozernov A., Murata T., Nelson D.R., Pils B.,
RA   Prigge M., Reiss B., Renner T., Rombauts S., Rushton P.J., Sanderfoot A.,
RA   Schween G., Shiu S.-H., Stueber K., Theodoulou F.L., Tu H., Van de Peer Y.,
RA   Verrier P.J., Waters E., Wood A., Yang L., Cove D., Cuming A.C., Hasebe M.,
RA   Lucas S., Mishler B.D., Reski R., Grigoriev I.V., Quatrano R.S.,
RA   Boore J.L.;
RT   "The Physcomitrella genome reveals evolutionary insights into the conquest
RT   of land by plants.";
RL   Science 319:64-69(2008).
RN   [2] {ECO:0000313|EMBL:PNR54396.1, ECO:0000313|Proteomes:UP000006727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Gransden 2004 {ECO:0000313|EnsemblPlants:Pp3c5_23480V3.1,
RC   ECO:0000313|Proteomes:UP000006727};
RX   PubMed=29237241; DOI=10.1111/tpj.13801;
RA   Lang D., Ullrich K.K., Murat F., Fuchs J., Jenkins J., Haas F.B.,
RA   Piednoel M., Gundlach H., Van Bel M., Meyberg R., Vives C., Morata J.,
RA   Symeonidi A., Hiss M., Muchero W., Kamisugi Y., Saleh O., Blanc G.,
RA   Decker E.L., van Gessel N., Grimwood J., Hayes R.D., Graham S.W.,
RA   Gunter L.E., McDaniel S.F., Hoernstein S.N.W., Larsson A., Li F.W.,
RA   Perroud P.F., Phillips J., Ranjan P., Rokshar D.S., Rothfels C.J.,
RA   Schneider L., Shu S., Stevenson D.W., Thummler F., Tillich M.,
RA   Villarreal Aguilar J.C., Widiez T., Wong G.K., Wymore A., Zhang Y.,
RA   Zimmer A.D., Quatrano R.S., Mayer K.F.X., Goodstein D., Casacuberta J.M.,
RA   Vandepoele K., Reski R., Cuming A.C., Tuskan G.A., Maumus F., Salse J.,
RA   Schmutz J., Rensing S.A.;
RT   "The Physcomitrella patens chromosome-scale assembly reveals moss genome
RT   structure and evolution.";
RL   Plant J. 93:515-533(2018).
RN   [3] {ECO:0000313|EnsemblPlants:Pp3c5_23480V3.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (DEC-2020) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC       family. {ECO:0000256|ARBA:ARBA00010044}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the AAA ATPase
CC       family. {ECO:0000256|ARBA:ARBA00010550}.
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DR   EMBL; ABEU02000005; PNR54396.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K1KKU2; -.
DR   STRING; 3218.A0A2K1KKU2; -.
DR   PaxDb; 3218-PP1S23_154V6-1; -.
DR   EnsemblPlants; Pp3c5_23480V3.1; Pp3c5_23480V3.1; Pp3c5_23480.
DR   EnsemblPlants; Pp3c5_23480V3.2; Pp3c5_23480V3.2; Pp3c5_23480.
DR   EnsemblPlants; Pp3c5_23480V3.3; Pp3c5_23480V3.3; Pp3c5_23480.
DR   EnsemblPlants; Pp3c5_23480V3.4; Pp3c5_23480V3.4; Pp3c5_23480.
DR   EnsemblPlants; Pp3c5_23480V3.5; Pp3c5_23480V3.5; Pp3c5_23480.
DR   Gramene; Pp3c5_23480V3.1; Pp3c5_23480V3.1; Pp3c5_23480.
DR   Gramene; Pp3c5_23480V3.2; Pp3c5_23480V3.2; Pp3c5_23480.
DR   Gramene; Pp3c5_23480V3.3; Pp3c5_23480V3.3; Pp3c5_23480.
DR   Gramene; Pp3c5_23480V3.4; Pp3c5_23480V3.4; Pp3c5_23480.
DR   Gramene; Pp3c5_23480V3.5; Pp3c5_23480V3.5; Pp3c5_23480.
DR   InParanoid; A0A2K1KKU2; -.
DR   OrthoDB; 9585at2759; -.
DR   Proteomes; UP000006727; Chromosome 5.
DR   GO; GO:0009534; C:chloroplast thylakoid; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0004176; F:ATP-dependent peptidase activity; IBA:GO_Central.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR   CDD; cd19501; RecA-like_FtsH; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.20.58.760; Peptidase M41; 1.
DR   HAMAP; MF_01458; FtsH; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041569; AAA_lid_3.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR003960; ATPase_AAA_CS.
DR   InterPro; IPR005936; FtsH.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR000642; Peptidase_M41.
DR   InterPro; IPR037219; Peptidase_M41-like.
DR   NCBIfam; TIGR01241; FtsH_fam; 1.
DR   PANTHER; PTHR23076:SF37; ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1; 1.
DR   PANTHER; PTHR23076; METALLOPROTEASE M41 FTSH; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF17862; AAA_lid_3; 1.
DR   Pfam; PF01434; Peptidase_M41; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF140990; FtsH protease domain-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS00674; AAA; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006727};
KW   Transit peptide {ECO:0000256|ARBA:ARBA00022946}.
FT   DOMAIN          277..413
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
SQ   SEQUENCE   729 AA;  78467 MW;  F381EFD1C54F4438 CRC64;
     MAWRLLMHEG SHVSKQLATS NALAGLGSHL KLSLYQLRLQ AISIENEGRR LLGCQRRQMS
     SYTSNYARRL EHAEGGSKLG SEDKQVSLLK QLNKVDPESV IQWFESRPSS HHSSAAMAEY
     VKALVKVDRL DESALLRTLQ QGAAIAGNGM RSETSMNVAS TAAPVLGSAG VMTKEGLLGT
     PQAPIHMVTA EGGLKVQAWR TLRTLALGFL LISGVGALIE DRGIGKGLGL NEEVQPSMES
     STKFSDVKGV DEAKAELEEI VHYLRDPQRF TSLGGKLPKG VLLVGPPGTG KTMLARAIAG
     EAGVPFFYCS GSEFEEMFVG VGARRVRDLF SAAKKRAPCI IFMDEIDAIG GSRNPKDQQY
     MKMTLNQLLV ELDGFKQNEG IIVVAATNFP ESLDKALVRP GRFDRHVVVP NPDVEGRRQI
     LEVHMSKVPK SGDVDLSIIA RGTPGFSGAD LANLINVAAL KAAMDGKKDV SMTDLEFAKD
     KIMMGSERKS AVISEESRRL TAYHEGGHAL VAIFTESALP VHKVTIVPRG MALGMVTQLP
     DKDETSFSRK QMLARLDVCM GGRVAEELVF GEGEVTSGAS SDIVRATKLA REMVTKYGMS
     KAVGVVAHNY EDDGKSMSTE TRLLVESEVR ELLQTAYENA KRILSTHQRE LHTLAATLLE
     RETMTAVEIK TLLAQVKEQA NRANIPLFSP QQIVPTTTAQ VAQAAAANAA AAVAAAASAK
     TKSAAPAGT
//
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