ID E3EK15_PAEPS Unreviewed; 595 AA.
AC E3EK15;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=PPSC2_26550 {ECO:0000313|EMBL:ADO59724.2};
OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OG Plasmid pSC2 {ECO:0000313|EMBL:ADO59724.2,
OG ECO:0000313|Proteomes:UP000006868}.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO59724.2, ECO:0000313|Proteomes:UP000006868};
RN [1] {ECO:0000313|EMBL:ADO59724.2, ECO:0000313|Proteomes:UP000006868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:ADO59724.2,
RC ECO:0000313|Proteomes:UP000006868};
RC PLASMID=pSC2 {ECO:0000313|Proteomes:UP000006868};
RX PubMed=21037012; DOI=10.1128/JB.01234-10;
RA Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT activity.";
RL J. Bacteriol. 193:311-312(2011).
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|RuleBase:RU003651}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the peptidase M41
CC family. {ECO:0000256|ARBA:ARBA00010044}.
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DR EMBL; CP002214; ADO59724.2; -; Genomic_DNA.
DR AlphaFoldDB; E3EK15; -.
DR KEGG; ppm:PPSC2_26550; -.
DR PATRIC; fig|886882.15.peg.5600; -.
DR eggNOG; COG0465; Bacteria.
DR HOGENOM; CLU_000688_16_2_9; -.
DR Proteomes; UP000006868; Plasmid pSC2.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 3.30.720.210; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.20.58.760; Peptidase M41; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
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 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; 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 ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Plasmid {ECO:0000313|EMBL:ADO59724.2};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000006868};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..125
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 193..329
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 137..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..151
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 595 AA; 65916 MW; 1F725780C331D2F9 CRC64;
MIKHRKKLIV LGILCAILIP LIMFLSNTPE PKKIQYTGFT KMLNEGKIKS VNIDFSLPSF
NFKDKKNQLY STDNPRRESF KDELLKKGVE VNESKKEGGL LQNILLALVN TLIWVAVFIG
LMTYLQKSMN GNSHIKEFDS AENENRGGKH SPKGSKRTTF KQIAGHEEAK EDMQYLVDFL
KNPLNYTIMG AKLPKGVIFY GPPGTGKTLF AKALAGEAGV PFFSVSGSDF VEKYVGTGAS
RVRDMFNLAR KKAPCIIFID EIDAIGRSRD SGSHSEQLQT LNAILKEMDG FDSNEGIIVI
GATNRLDDLD SAFIRPGRFD KHIAIHLPDQ KSRLDILKIH AQNKPLATDV DLESLSKLTV
GLSGASLESI LNESSILATS RRQKEITAKE IDDAYFKIVM QGHKKKGGDK RHKDEIRLVS
WHEAGHALAS KLLTDNDVPK VTIIPSTSGA GGVAFIIPKK MGLNSKRDLI NDIKISYAGR
AAEYLLLGNH MEITTGASSD IKNATKKIKM MITEVGMSDA FGMLNLDEFK PDYQSILDEA
STLAKQLYDE TVELLTKHLV TLKAIAEALE QKESLNEDEL NTIIEKTQNE VVEAC
//
