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Multifunctional fusion protein [Includes: ATP-dependent Clp protease ATP-binding subunit ClpX; Lon protease (EC 3.4.21.53) (ATP-dependent protease La)]

 W9T9W7_9PSED            Unreviewed;      1268 AA.
W9T9W7;
14-MAY-2014, integrated into UniProtKB/TrEMBL.
14-MAY-2014, sequence version 1.
18-JUL-2018, entry version 35.
RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|HAMAP-Rule:MF_01973};
Includes:
RecName: Full=ATP-dependent Clp protease ATP-binding subunit ClpX {ECO:0000256|HAMAP-Rule:MF_00175};
Includes:
RecName: Full=Lon protease {ECO:0000256|HAMAP-Rule:MF_01973};
EC=3.4.21.53 {ECO:0000256|HAMAP-Rule:MF_01973};
AltName: Full=ATP-dependent protease La {ECO:0000256|HAMAP-Rule:MF_01973};
Name=lon {ECO:0000256|HAMAP-Rule:MF_01973,
ECO:0000313|EMBL:EXF47248.1};
Synonyms=clpX {ECO:0000256|HAMAP-Rule:MF_00175};
ORFNames=BAY1663_00266 {ECO:0000313|EMBL:EXF47248.1};
Pseudomonas sp. BAY1663.
Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
Pseudomonadaceae; Pseudomonas.
NCBI_TaxID=1439940 {ECO:0000313|EMBL:EXF47248.1, ECO:0000313|Proteomes:UP000019475};
[1] {ECO:0000313|EMBL:EXF47248.1, ECO:0000313|Proteomes:UP000019475}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=BAY1663 {ECO:0000313|EMBL:EXF47248.1,
ECO:0000313|Proteomes:UP000019475};
Gyula P., Szabo Z., Robotka H., Bihari Z.;
"Genome sequencing of Pseudomonas sp. BAY1663.";
Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: ATP-dependent serine protease that mediates the
selective degradation of mutant and abnormal proteins as well as
certain short-lived regulatory proteins. Required for cellular
homeostasis and for survival from DNA damage and developmental
changes induced by stress. Degrades polypeptides processively to
yield small peptide fragments that are 5 to 10 amino acids long.
Binds to DNA in a double-stranded, site-specific manner.
{ECO:0000256|HAMAP-Rule:MF_01973}.
-!- FUNCTION: ATP-dependent specificity component of the Clp protease.
It directs the protease to specific substrates. Can perform
chaperone functions in the absence of ClpP. {ECO:0000256|HAMAP-
Rule:MF_00175, ECO:0000256|SAAS:SAAS01014585}.
-!- CATALYTIC ACTIVITY: Hydrolysis of proteins in presence of ATP.
{ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|SAAS:SAAS00338825}.
-!- SUBUNIT: Component of the ClpX-ClpP complex. Forms a hexameric
ring that, in the presence of ATP, binds to fourteen ClpP subunits
assembled into a disk-like structure with a central cavity,
resembling the structure of eukaryotic proteasomes.
{ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS00645732}.
-!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity.
{ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|SAAS:SAAS00536021}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973,
ECO:0000256|SAAS:SAAS00007367}.
-!- INDUCTION: By heat shock. {ECO:0000256|HAMAP-Rule:MF_01973}.
-!- SIMILARITY: Belongs to the ClpX chaperone family.
{ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS00701777}.
-!- SIMILARITY: Belongs to the peptidase S16 family.
{ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PROSITE-
ProRule:PRU01122, ECO:0000256|SAAS:SAAS00536024}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EXF47248.1}.
-----------------------------------------------------------------------
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EMBL; AZSV01000002; EXF47248.1; -; Genomic_DNA.
EnsemblBacteria; EXF47248; EXF47248; BAY1663_00266.
PATRIC; fig|1439940.3.peg.264; -.
Proteomes; UP000019475; Unassembled WGS sequence.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:UniProtKB-UniRule.
GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
GO; GO:0043565; F:sequence-specific DNA binding; IEA:UniProtKB-UniRule.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
GO; GO:0051082; F:unfolded protein binding; IEA:UniProtKB-UniRule.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0033554; P:cellular response to stress; IEA:UniProtKB-UniRule.
GO; GO:0006457; P:protein folding; IEA:UniProtKB-UniRule.
GO; GO:0006515; P:protein quality control for misfolded or incompletely synthesized proteins; IEA:UniProtKB-UniRule.
Gene3D; 3.30.230.10; -; 1.
Gene3D; 3.30.50.30; -; 1.
HAMAP; MF_00175; ClpX; 1.
HAMAP; MF_01973; lon_bact; 1.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR019489; Clp_ATPase_C.
InterPro; IPR004487; Clp_protease_ATP-bd_su_ClpX.
InterPro; IPR027543; Lon_bac.
InterPro; IPR004815; Lon_bac/euk-typ.
InterPro; IPR008269; Lon_proteolytic.
InterPro; IPR027065; Lon_Prtase.
InterPro; IPR003111; Lon_substr-bd.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR015947; PUA-like_sf.
InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
InterPro; IPR010603; Znf_CppX_C4.
InterPro; IPR038366; Znf_CppX_C4_sf.
PANTHER; PTHR10046; PTHR10046; 1.
Pfam; PF00004; AAA; 1.
Pfam; PF07724; AAA_2; 1.
Pfam; PF10431; ClpB_D2-small; 1.
Pfam; PF05362; Lon_C; 1.
Pfam; PF02190; LON_substr_bdg; 1.
Pfam; PF06689; zf-C4_ClpX; 1.
SMART; SM00382; AAA; 2.
SMART; SM01086; ClpB_D2-small; 1.
SMART; SM00464; LON; 1.
SMART; SM00994; zf-C4_ClpX; 1.
SUPFAM; SSF52540; SSF52540; 2.
SUPFAM; SSF54211; SSF54211; 1.
SUPFAM; SSF88697; SSF88697; 1.
TIGRFAMs; TIGR00382; clpX; 1.
TIGRFAMs; TIGR00763; lon; 1.
PROSITE; PS51787; LON_N; 1.
PROSITE; PS51786; LON_PROTEOLYTIC; 1.
2: Evidence at transcript level;
ATP-binding {ECO:0000256|HAMAP-Rule:MF_00175,
ECO:0000256|SAAS:SAAS00701780};
Chaperone {ECO:0000256|HAMAP-Rule:MF_00175,
ECO:0000256|SAAS:SAAS00645733};
Complete proteome {ECO:0000313|Proteomes:UP000019475};
Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01973,
ECO:0000256|SAAS:SAAS00004285};
Hydrolase {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PROSITE-
ProRule:PRU01122, ECO:0000256|SAAS:SAAS00004356};
Metal-binding {ECO:0000256|HAMAP-Rule:MF_00175,
ECO:0000256|SAAS:SAAS00645738};
Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00175,
ECO:0000256|SAAS:SAAS00701780};
Protease {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PROSITE-
ProRule:PRU01122, ECO:0000256|SAAS:SAAS00004356};
Reference proteome {ECO:0000313|Proteomes:UP000019475};
Serine protease {ECO:0000256|HAMAP-Rule:MF_01973, ECO:0000256|PROSITE-
ProRule:PRU01122, ECO:0000256|SAAS:SAAS00004356};
Stress response {ECO:0000256|HAMAP-Rule:MF_01973,
ECO:0000256|SAAS:SAAS00004281};
Zinc {ECO:0000256|HAMAP-Rule:MF_00175, ECO:0000256|SAAS:SAAS00645738};
Zinc-finger {ECO:0000256|HAMAP-Rule:MF_00175,
ECO:0000256|SAAS:SAAS00645738}.
DOMAIN 477 668 Lon N-terminal.
{ECO:0000259|PROSITE:PS51787}.
DOMAIN 1057 1238 Lon proteolytic.
{ECO:0000259|PROSITE:PS51786}.
ZN_FING 16 41 C4-type. {ECO:0000256|HAMAP-
Rule:MF_00175}.
NP_BIND 121 128 ATP. {ECO:0000256|HAMAP-Rule:MF_00175}.
NP_BIND 822 829 ATP. {ECO:0000256|HAMAP-Rule:MF_01973}.
ACT_SITE 1144 1144 {ECO:0000256|HAMAP-Rule:MF_01973,
ECO:0000256|PROSITE-ProRule:PRU01122}.
ACT_SITE 1187 1187 {ECO:0000256|HAMAP-Rule:MF_01973,
ECO:0000256|PROSITE-ProRule:PRU01122}.
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


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