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Database: UniProt
Entry: A0A1W2C5C3_9SPHN
LinkDB: A0A1W2C5C3_9SPHN
Original site: A0A1W2C5C3_9SPHN 
ID   A0A1W2C5C3_9SPHN        Unreviewed;       791 AA.
AC   A0A1W2C5C3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=ATP-dependent Clp protease ATP-binding subunit ClpA {ECO:0000313|EMBL:SMC80455.1};
GN   ORFNames=SAMN06272759_107179 {ECO:0000313|EMBL:SMC80455.1};
OS   Novosphingobium sp. B1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1938756 {ECO:0000313|EMBL:SMC80455.1, ECO:0000313|Proteomes:UP000192500};
RN   [1] {ECO:0000313|Proteomes:UP000192500}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B1 {ECO:0000313|Proteomes:UP000192500};
RA   Varghese N., Submissions S.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; FWXL01000007; SMC80455.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W2C5C3; -.
DR   STRING; 1938756.SAMN06272759_107179; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000192500; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0043335; P:protein unfolding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 2.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003959; ATPase_AAA_core.
DR   InterPro; IPR019489; Clp_ATPase_C.
DR   InterPro; IPR036628; Clp_N_dom_sf.
DR   InterPro; IPR004176; Clp_R_dom.
DR   InterPro; IPR013461; ClpA.
DR   InterPro; IPR001270; ClpA/B.
DR   InterPro; IPR018368; ClpA/B_CS1.
DR   InterPro; IPR028299; ClpA/B_CS2.
DR   InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR02639; ClpA; 1.
DR   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF111; ATP-DEPENDENT CLP PROTEASE ATP-BINDING SUBUNIT CLPA; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 1.
DR   Pfam; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF81923; Double Clp-N motif; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   PROSITE; PS51903; CLP_R; 1.
DR   PROSITE; PS00870; CLPAB_1; 1.
DR   PROSITE; PS00871; CLPAB_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW   Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW   Hydrolase {ECO:0000313|EMBL:SMC80455.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:SMC80455.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          1..146
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          144..177
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          769..791
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        152..177
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   791 AA;  86877 MW;  108AD43B6E8AAE88 CRC64;
     MPSFAQSLEK TLHTALANAS ERSHEYATLE HLLLALIDDP DAAQVMQACG VDLGDLGDVV
     RQYLDQEYQS LKTQEKADPQ PTAGFQRVIQ RAILHVQSSG KDTVTGANVL VALFSERDSY
     AVYFLQQQDM SRLDAVSFIS HGIGKGGRQV DGRTPKGAEE EAPKQQEEKA DAKGQKKETA
     LDQFTVNLNE KALGGKVDPL IGRGPEVDRT IQILCRRSKN NPLYVGDPGV GKTAIAEGLA
     RKIVEGEVPE VLAEAVIYSL DMGSLLAGTR YRGDFEERLK QVVSELEKMP HAVLFIDEIH
     TVIGAGATSG GAMDASNLLK PALSGGTIRC IGSTTYKEFR NHFEKDRALL RRFQKIDVNE
     PTIEDTIKIL RGLRTAFEEH HKVKYTPDAI KTAVELSARY INDRKLPDKA IDVIDEVGAM
     QMLVPPNKRK KTITAREIEQ VIATMARIPP KSVSSDDKKV LEHLERDLKR LVFGQDKAIE
     VLSSAMKLSR AGLRDPDKPI GSFLFSGPTG VGKTEVARSL AQIMGIPLQR FDMSEYMERH
     SVSRLIGAPP GYVGFDQGGL LTDAIDQQPH CVLLLDEIEK AHPDLFNILL QVMDNGRLTD
     HHGKTVDFRN VVLIMTTNAG ASDMARQGIG FGDVSKADAG DEAVKKMFTP EFRNRLDAIV
     PFGYLPPEVV SRVVDKFVLQ LELQLAEQNV HIQFDADARS WLAKKGYDKL YGARPMARLI
     QEKVKKPLAE ELLFGKLANG GEVHVSLKQE DGQDGALSFE LTPAAPKLVK KKARKGKAGS
     AAPETSADEA E
//
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