ID W9T9W7_9PSED Unreviewed; 1268 AA.
AC W9T9W7;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 64.
DE RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|HAMAP-Rule:MF_01973};
DE Includes:
DE RecName: Full=Lon protease {ECO:0000256|HAMAP-Rule:MF_01973};
DE EC=3.4.21.53 {ECO:0000256|HAMAP-Rule:MF_01973};
DE AltName: Full=ATP-dependent protease La {ECO:0000256|HAMAP-Rule:MF_01973};
DE Includes:
DE RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000256|HAMAP-Rule:MF_00175};
GN Name=lon {ECO:0000256|HAMAP-Rule:MF_01973,
GN ECO:0000313|EMBL:EXF47248.1};
GN Synonyms=clpX {ECO:0000256|HAMAP-Rule:MF_00175};
GN ORFNames=BAY1663_00266 {ECO:0000313|EMBL:EXF47248.1};
OS Pseudomonas sp. BAY1663.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1439940 {ECO:0000313|EMBL:EXF47248.1, ECO:0000313|Proteomes:UP000019475};
RN [1] {ECO:0000313|EMBL:EXF47248.1, ECO:0000313|Proteomes:UP000019475}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAY1663 {ECO:0000313|EMBL:EXF47248.1,
RC ECO:0000313|Proteomes:UP000019475};
RA Gyula P., Szabo Z., Robotka H., Bihari Z.;
RT "Genome sequencing of Pseudomonas sp. BAY1663.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent serine protease that mediates the selective
CC degradation of mutant and abnormal proteins as well as certain short-
CC lived regulatory proteins. Required for cellular homeostasis and for
CC survival from DNA damage and developmental changes induced by stress.
CC Degrades polypeptides processively to yield small peptide fragments
CC that are 5 to 10 amino acids long. Binds to DNA in a double-stranded,
CC site-specific manner. {ECO:0000256|HAMAP-Rule:MF_01973}.
CC -!- FUNCTION: ATP-dependent specificity component of the Clp protease. It
CC directs the protease to specific substrates. Can perform chaperone
CC functions in the absence of ClpP. {ECO:0000256|HAMAP-Rule:MF_00175}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of proteins in presence of ATP.; EC=3.4.21.53;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PROSITE-
CC ProRule:PRU01122};
CC -!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric ring
CC that, in the presence of ATP, binds to fourteen ClpP subunits assembled
CC into a disk-like structure with a central cavity, resembling the
CC structure of eukaryotic proteasomes. {ECO:0000256|HAMAP-Rule:MF_00175}.
CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
CC {ECO:0000256|HAMAP-Rule:MF_01973}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_01973}.
CC -!- INDUCTION: By heat shock. {ECO:0000256|HAMAP-Rule:MF_01973}.
CC -!- SIMILARITY: Belongs to the ClpX chaperone family. {ECO:0000256|HAMAP-
CC Rule:MF_00175, ECO:0000256|PROSITE-ProRule:PRU01250}.
CC -!- SIMILARITY: Belongs to the peptidase S16 family. {ECO:0000256|HAMAP-
CC Rule:MF_01973, ECO:0000256|PROSITE-ProRule:PRU01122}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EXF47248.1}.
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DR EMBL; AZSV01000002; EXF47248.1; -; Genomic_DNA.
DR AlphaFoldDB; W9T9W7; -.
DR STRING; 1439940.BAY1663_00266; -.
DR PATRIC; fig|1439940.3.peg.264; -.
DR eggNOG; COG0466; Bacteria.
DR eggNOG; COG1219; Bacteria.
DR Proteomes; UP000019475; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0140662; F:ATP-dependent protein folding chaperone; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0034605; P:cellular response to heat; IEA:UniProtKB-UniRule.
DR GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
DR CDD; cd19497; RecA-like_ClpX; 1.
DR CDD; cd19500; RecA-like_Lon; 1.
DR Gene3D; 1.10.8.60; -; 2.
DR Gene3D; 1.20.5.5270; -; 1.
DR Gene3D; 1.20.58.1480; -; 1.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 6.20.220.10; ClpX chaperone, C4-type zinc finger domain; 1.
DR Gene3D; 2.30.130.40; LON domain-like; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR HAMAP; MF_00175; ClpX; 1.
DR HAMAP; MF_01973; lon_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
DR InterPro; IPR046425; ClpX_bact.
DR InterPro; IPR027543; Lon_bac.
DR InterPro; IPR004815; Lon_bac/euk-typ.
DR InterPro; IPR008269; Lon_proteolytic.
DR InterPro; IPR027065; Lon_Prtase.
DR InterPro; IPR003111; Lon_prtase_N.
DR InterPro; IPR046336; Lon_prtase_N_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR InterPro; IPR010603; Znf_CppX_C4.
DR InterPro; IPR038366; Znf_CppX_C4_sf.
DR NCBIfam; TIGR00382; clpX; 1.
DR NCBIfam; TIGR00763; lon; 1.
DR PANTHER; PTHR10046; ATP DEPENDENT LON PROTEASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10046:SF56; LON PROTEASE; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR Pfam; PF05362; Lon_C; 1.
DR Pfam; PF02190; LON_substr_bdg; 1.
DR Pfam; PF06689; zf-C4_ClpX; 1.
DR PRINTS; PR00830; ENDOLAPTASE.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SMART; SM00464; LON; 1.
DR SMART; SM00994; zf-C4_ClpX; 1.
DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR SUPFAM; SSF88697; PUA domain-like; 1.
DR SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR PROSITE; PS51902; CLPX_ZB; 1.
DR PROSITE; PS51787; LON_N; 1.
DR PROSITE; PS51786; LON_PROTEOLYTIC; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00175};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_00175};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PROSITE-
KW ProRule:PRU01122};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00175};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00175};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01973};
KW Reference proteome {ECO:0000313|Proteomes:UP000019475};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|HAMAP-
KW Rule:MF_01973}; Stress response {ECO:0000256|HAMAP-Rule:MF_01973};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00175}.
FT DOMAIN 4..57
FT /note="ClpX-type ZB"
FT /evidence="ECO:0000259|PROSITE:PS51902"
FT DOMAIN 477..668
FT /note="Lon N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51787"
FT DOMAIN 1057..1238
FT /note="Lon proteolytic"
FT /evidence="ECO:0000259|PROSITE:PS51786"
FT REGION 1246..1268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1248..1268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1144
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT ACT_SITE 1187
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973,
FT ECO:0000256|PROSITE-ProRule:PRU01122"
FT BINDING 16
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 19
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 41
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175,
FT ECO:0000256|PROSITE-ProRule:PRU01250"
FT BINDING 121..128
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00175"
FT BINDING 822..829
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01973"
SQ SEQUENCE 1268 AA; 140527 MW; 4CB8354A6B187992 CRC64;
MTDTRNGEDS GKLLYCSFCG KSQHEVRKLI AGPSVFICDE CVDLCNDIIR EEVQEAQAES
SAHKLPAPKE ISGILDQYVI GQERAKKILA VAVYNHYKRL NQRDKKEEVE LGKSNILLIG
PTGSGKTLLA ETLARLLNVP FTIADATTLT EAGYVGEDVE NIIQKLLQKC DYDVEKAQMG
IVYIDEIDKI SRKSDNPSIT RDVSGEGVQQ ALLKLIEGTV ASVPPQGGRK HPQQEFLQVD
TRNILFICGG AFAGLEKVIQ GRSTQGGIGF NAEVRSKDPG KKIGEALRSV EPDDLVKFGL
IPEFVGRLPV IATLDELDEA ALIQILTEPK NALTKQYAKL FELEGVDLEF RPDALKAVAQ
RALERKTGAR GLRSILEGVL LDTMYDIPSQ KDVSKVVIDE SVIEGTSQPL LIYENSEPPA
KLRLRRDRTK GPAGPFVFVP SPCFLQGMPS SLQQGYSVRL PPYGRRRAEF MKTTIELPLL
PLRDVVVYPH MVIPLFVGRE KSIEALESAM AGDKQILLLA QKNPADDDPV EDALYRVGTV
ATVLQLLKLP DGTVKVLVEG EQRGVIERFL EVDDHCRAEV ALIEESEVEA RESEVFTRSL
LSQFEQYVQL GKKVPAEVLS SLSSIDEPAR LVDTMAAHMA LKIEQKQEIL EITELPARVE
HVLALLDAEI DLLQVEKRIR GRVKKQMERS QREYYLNEQM KAIQKELGDI DEGHNEIDDL
KKRIENAGLS KDAYAKAQAE LNKLKQMSPM SAEATVVRTY IDWLVNVPWK AASKVRLDLG
KAEEVLDADH YGLEEVKDRI LEYLAVQKRV KKLKGPVLCL VGPPGVGKTS LAESIARSTN
RKFVRMALGG VRDEAEIRGH RRTYIGSMPG RLIQKMTKVG VRNPLFLLDE IDKMGSDMRG
DPASALLEVL DPEQNHNFND HYLEVDYDLS DVMFLCTANS MNIPAPLLDR MEVIRLPGYT
EDEKVNIATR YLAPKQIQAN GLKKGEVEFE EAAIRDIIRY YTREAGVRSL ERQLAKVCRK
VVKEHAAQKR FQVTVGADSL EHFLGVRKFR YGLAELQDQV GQVTGLAWTQ VGGELLTIEA
AVVPGKGRLT KTGSLGEVMG ESITAALTVV RSRATSLGIA VDFHEKQDIH IHVPEGATPK
DGPSAGIGMC TALVSALTQI PVRADVAMTG EITLRGQVLA IGGLKEKLLA AHRGGIKTVI
IPEENQRDLK EIPENIKQDL QIKPVKWIDE VLQIALQYAP EPLPDAAPEI VAKDDKREPD
SKERISTH
//