ID R7Q3R0_CHOCR Unreviewed; 888 AA.
AC R7Q3R0;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE SubName: Full=ATP-dependent Zn protease FtsH2 {ECO:0000313|EMBL:CDF33172.1};
GN ORFNames=CHC_T00009243001 {ECO:0000313|EMBL:CDF33172.1};
OS Chondrus crispus (Carrageen Irish moss) (Polymorpha crispa).
OC Eukaryota; Rhodophyta; Florideophyceae; Rhodymeniophycidae; Gigartinales;
OC Gigartinaceae; Chondrus.
OX NCBI_TaxID=2769 {ECO:0000313|EMBL:CDF33172.1, ECO:0000313|Proteomes:UP000012073};
RN [1] {ECO:0000313|Proteomes:UP000012073}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Stackhouse {ECO:0000313|Proteomes:UP000012073};
RX PubMed=23503846; DOI=10.1073/pnas.1221259110;
RA Collen J., Porcel B., Carre W., Ball S.G., Chaparro C., Tonon T.,
RA Barbeyron T., Michel G., Noel B., Valentin K., Elias M., Artiguenave F.,
RA Arun A., Aury J.M., Barbosa-Neto J.F., Bothwell J.H., Bouget F.Y.,
RA Brillet L., Cabello-Hurtado F., Capella-Gutierrez S., Charrier B.,
RA Cladiere L., Cock J.M., Coelho S.M., Colleoni C., Czjzek M., Da Silva C.,
RA Delage L., Denoeud F., Deschamps P., Dittami S.M., Gabaldon T.,
RA Gachon C.M., Groisillier A., Herve C., Jabbari K., Katinka M., Kloareg B.,
RA Kowalczyk N., Labadie K., Leblanc C., Lopez P.J., McLachlan D.H.,
RA Meslet-Cladiere L., Moustafa A., Nehr Z., Nyvall Collen P., Panaud O.,
RA Partensky F., Poulain J., Rensing S.A., Rousvoal S., Samson G.,
RA Symeonidi A., Weissenbach J., Zambounis A., Wincker P., Boyen C.;
RT "Genome structure and metabolic features in the red seaweed Chondrus
RT crispus shed light on evolution of the Archaeplastida.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:5247-5252(2013).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast
CC {ECO:0000256|ARBA:ARBA00004229}.
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; HG001635; CDF33172.1; -; Genomic_DNA.
DR RefSeq; XP_005712975.1; XM_005712918.1.
DR AlphaFoldDB; R7Q3R0; -.
DR STRING; 2769.R7Q3R0; -.
DR MEROPS; M41.A17; -.
DR EnsemblPlants; CDF33172; CDF33172; CHC_T00009243001.
DR GeneID; 17320683; -.
DR Gramene; CDF33172; CDF33172; CHC_T00009243001.
DR KEGG; ccp:CHC_T00009243001; -.
DR OMA; ARQKGNF; -.
DR OrthoDB; 9585at2759; -.
DR PhylomeDB; R7Q3R0; -.
DR Proteomes; UP000012073; Unassembled WGS sequence.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
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; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; 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; 3.40.1690.20; -; 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; IPR011546; Pept_M41_FtsH_extracell.
DR InterPro; IPR000642; Peptidase_M41.
DR InterPro; IPR037219; Peptidase_M41-like.
DR NCBIfam; TIGR01241; FtsH_fam; 1.
DR PANTHER; PTHR43655; ATP-DEPENDENT PROTEASE; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF06480; FtsH_ext; 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 Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:CDF33172.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000012073}.
FT DOMAIN 290..430
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 711..769
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 711..730
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 888 AA; 96568 MW; 9D037A122B7CA8B5 CRC64;
MTEDHPRKPT ASKGKTGPGA ENGDPKGPEA KADNVAGGGG GGNKEGGKTD GPGKPGKPQS
DDDQSNSWMG QAALALFVML GLSLLGSRDH GREISFQAFV WDLLEPGLVD RIEVVNRNVA
RVYLRTSARA RPQDAAFETR RGQRGSMATI NSTESPFYFN IGTIDTFERK LEAVQEDLGI
EPDDLVPVVY TKESSLTTEL LRQAPSIILL GIGILVLRNA LGQLGGMGGG RSGIFQVGKA
NPTVVKGGEA GVQTTTFSQV AGLDEAKLEV MEFVDFLKNP ARYEKLGAKI PKGALLVGPP
GTGKTLLARA TAGEANVPFF SMSGSDFIEM FVGVGPSRVR DLFTQARASA PCIIFIDEID
AIGKARGRSG ISGGNDEREN TLNALLVEMD GFSSSAGVVV LAGTNRADVL DKALLRPGRF
DRQISIDKPD MRGRYQIFMV HLQPLKLKDE ASKIAKRLAA LSPGFAGADI ANICNEAALI
AARQDKNFIE MIDFEKAIDR VIGGLEKKNK VISRKEREIV AHHEAGHAVA GWFLKHADPL
IKVSIIPRGS AALGFAQYLP VDKFLQSREQ MKDFMIMALG GRVAEQLCFG SITTGAQDDL
KRITRAVYAQ ITTFGMSEKV GKIYFPKAGE SGNQFYKPYS EKTAELIDDE ALRIVEEAYL
DCEKLLTEKL DVVKNLATRL LDKEVIGEED LIDVLGPRPF AKPATYDELV GRYEQDRKKR
TGKGGENDDP SARDPSTTPP IPVEGAPAGA PTGQGFKRRG HTRPTPDEEA IPELAAIVAH
FVFSSTRWKM PPAPLQWSPF LPRYFAYLSM VAIASIWQSD IFYPSDKSDY SSHCQDKKSR
TESCSKKDFI DLCFLAITDE PVHRHIGLYC QQRHSPKCCC SNIGSKAK
//
