ID A0A073CAU5_PLAAG Unreviewed; 378 AA.
AC A0A073CAU5;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=FtsH {ECO:0000313|EMBL:KEI65226.1};
DE EC=3.6.4.6 {ECO:0000313|EMBL:KEI65226.1};
GN Name=ftsH {ECO:0000313|EMBL:KEI65226.1};
GN ORFNames=A19Y_9017 {ECO:0000313|EMBL:KEI65226.1};
OS Planktothrix agardhii NIVA-CYA 126/8.
OG Plasmid pPA115 {ECO:0000313|EMBL:KEI65226.1,
OG ECO:0000313|Proteomes:UP000027395}.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Planktothrix.
OX NCBI_TaxID=388467 {ECO:0000313|EMBL:KEI65226.1, ECO:0000313|Proteomes:UP000027395};
RN [1] {ECO:0000313|EMBL:KEI65226.1, ECO:0000313|Proteomes:UP000027395}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIVA-CYA 126/8 {ECO:0000313|EMBL:KEI65226.1,
RC ECO:0000313|Proteomes:UP000027395};
RC PLASMID=pPA115 {ECO:0000313|EMBL:KEI65226.1};
RX PubMed=24907328; DOI=10.1128/AEM.01188-14;
RA Christiansen G., Goesmann A., Kurmayer R.;
RT "Elucidation of insertion elements encoded on plasmids and in vitro
RT construction of shuttle vectors from the toxic cyanobacterium
RT Planktothrix.";
RL Appl. Environ. Microbiol. 80:4887-4897(2014).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914}.
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; CM002804; KEI65226.1; -; Genomic_DNA.
DR RefSeq; WP_042158358.1; NZ_CM002804.1.
DR AlphaFoldDB; A0A073CAU5; -.
DR PATRIC; fig|388467.6.peg.4642; -.
DR HOGENOM; CLU_000688_25_2_3; -.
DR Proteomes; UP000027395; Plasmid pPA115.
DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd19481; RecA-like_protease; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR23073:SF155; 26S PROTEASOME REGULATORY SUBUNIT 10B; 1.
DR Pfam; PF00004; AAA; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:KEI65226.1};
KW Plasmid {ECO:0000313|EMBL:KEI65226.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027395}.
FT DOMAIN 129..263
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 45..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 337..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..378
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 378 AA; 41635 MW; 3E1EDA0C454F08E3 CRC64;
MANLVIRGMP QGISETTAAV CRSRLLRDVG DMLTETGLKD VEITVTTSPN SNSSPKQVGN
NRSDSNEEGK EFSVEKLAEK YESDQPLYKF DQLVVGDDLR EDLLSAIDLI RVEPKVFDEW
GLRIIEPFPR TALNFHGAPG TGKTLAAHAI ANKLDKKILL ASYAAIESPL LGVGTKNLEA
VFYAASRDNA VLFLDEADSL LSKRITSVSQ GSERAANAMC SQLLICLEKF HGVVIFATNL
VENYDRAFET RVRHIQFPMP NTEARAVIWR KHLPGKLPLA ANVSIENLAE IEDVCGRDIK
NAVIDAAIRT ARNNKECVEM QELVEAVNRI KSARISVSGN SRKLTPEEEA KVKEKLKEAL
SKQENASNQE NNGSSEKS
//