ID A0A1U7WCC6_NICSY Unreviewed; 707 AA.
AC A0A1U7WCC6;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=ATP-dependent zinc metalloprotease FTSH, chloroplastic {ECO:0000313|RefSeq:XP_009777632.1};
GN Name=LOC104227163 {ECO:0000313|RefSeq:XP_009777632.1};
OS Nicotiana sylvestris (Wood tobacco) (South American tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4096 {ECO:0000313|Proteomes:UP000189701, ECO:0000313|RefSeq:XP_009777632.1};
RN [1] {ECO:0000313|Proteomes:UP000189701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23773524; DOI=10.1186/gb-2013-14-6-r60;
RA Sierro N., Battey J.N., Ouadi S., Bovet L., Goepfert S., Bakaher N.,
RA Peitsch M.C., Ivanov N.V.;
RT "Reference genomes and transcriptomes of Nicotiana sylvestris and Nicotiana
RT tomentosiformis.";
RL Genome Biol. 14:R60.1-R60.17(2013).
RN [2] {ECO:0000313|RefSeq:XP_009777632.1}
RP IDENTIFICATION.
RC TISSUE=Leaf {ECO:0000313|RefSeq:XP_009777632.1};
RG RefSeq;
RL Submitted (NOV-2023) 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 RefSeq; XP_009777632.1; XM_009779330.1.
DR AlphaFoldDB; A0A1U7WCC6; -.
DR STRING; 4096.A0A1U7WCC6; -.
DR GeneID; 104227163; -.
DR KEGG; nsy:104227163; -.
DR eggNOG; KOG0731; Eukaryota.
DR OrthoDB; 9585at2759; -.
DR Proteomes; UP000189701; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IEA:UniProt.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd19501; RecA-like_FtsH; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.30.720.210; -; 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:SF97; ATP-DEPENDENT ZINC METALLOPROTEASE FTSH 2, CHLOROPLASTIC-RELATED; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000313|RefSeq:XP_009777632.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000189701};
KW Transit peptide {ECO:0000256|ARBA:ARBA00022946};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 285..424
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
SQ SEQUENCE 707 AA; 76104 MW; 4673DE722835D185 CRC64;
MANSLLSSNF MGSQIFVSPP TPKTTKYFHF HSKRKSLIPQ SILNKKPNSD NSKNIPSKAA
LAALLFSSIT PHAYALDNTT PTVPTPQVIQ AEAANPTTSN PFSQNIILNA PKPQAQTNPE
LPEVSQWRYS EFLNAVKKGK VERVRFSKDG TTLQLNAVDG RRASVIVPND PDLIDILAMN
GVDISVSEGD SGGNGLFNLI GSLFPFIAFA GLFYLFQRSQ GGPGGPGGLG GPMDFGRSKS
KFQEVPETGV SFADVAGADQ AKLELQEVVD FLKNPDKYTA LGAKIPKGCL LVGPPGTGKT
LLARAVAGEA GVPFFSCAAS EFVELFVGVG ASRVRDLFEK AKSKAPCIVF IDEIDAVGRQ
RGAGMGGGND EREQTINQLL TEMDGFSGNS GVIVLAATNR PDVLDSALLR PGRFDRQVTV
DRPDVAGRIK ILQVHSRGKA LAKDVDFEKI ARRTPGFTGA DLQNLMNEAA ILAARRELKE
ISKDEISDAL ERIIAGPEKK NAVVSEEKKK LVAYHEAGHA LVGALMPEYD PVAKISIIPR
GQAGGLTFFA PSEERLESGL YSRSYLENQM AVALGGRVAE EVIFGQDNVT TGASNDFMQV
SRVARQMVER LGFSKKIGQV AIGGGGGNPF LGQQMSTQKD YSMATADVVD AEVRELVERA
YERATQIITT HIDILHKLAQ LLIEKETVDG EEFMSLFIDG KAELYIS
//
