ID A1S7A5_SHEAM Unreviewed; 753 AA.
AC A1S7A5;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 24-JAN-2024, entry version 99.
DE SubName: Full=ATP-dependent Clp protease, ATP-binding subunit ClpA {ECO:0000313|EMBL:ABM00262.1};
GN OrderedLocusNames=Sama_2056 {ECO:0000313|EMBL:ABM00262.1};
OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=326297 {ECO:0000313|EMBL:ABM00262.1, ECO:0000313|Proteomes:UP000009175};
RN [1] {ECO:0000313|EMBL:ABM00262.1, ECO:0000313|Proteomes:UP000009175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1098 / SB2B {ECO:0000313|Proteomes:UP000009175};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA Richardson P.;
RT "Complete sequence of Shewanella amazonensis SB2B.";
RL Submitted (DEC-2006) 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; CP000507; ABM00262.1; -; Genomic_DNA.
DR RefSeq; WP_011760169.1; NC_008700.1.
DR AlphaFoldDB; A1S7A5; -.
DR STRING; 326297.Sama_2056; -.
DR KEGG; saz:Sama_2056; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_2_6; -.
DR OMA; GRVIQEH; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000009175; Chromosome.
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:ABM00262.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432}; Protease {ECO:0000313|EMBL:ABM00262.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000009175};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}.
FT DOMAIN 1..145
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 143..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 753 AA; 83325 MW; C2E5EBBC39B9911F CRC64;
MLNKDLEVTL NLAFQQARDA RHEYMTVEHL LLALIDNPSA QDALVACGAN IDKLREEVAT
FISQTTPVIT DPDDDRETQP TLGFQRVLQR AVFHVQSSGR NEVTGANVLV AIFSEQESQA
VYLLRRSDIT RLDVVNYISH GFSKSEDAPQ ESEQERIEDH SEQGEEQRSM LSQFAANLNL
LAAQGVIDPL IGRDNEIERS IQILCRRRKN NPLLVGEAGV GKTAIAEGLA YRIVNDDVPE
VMRDATVYSL DLGALLAGTK YRGDFEKRFK SLLKELTADK HAILFIDEIH TIIGAGAASG
GVMDASNLLK PLLSSGTLRC MGSTTFQEYQ SIFEKDRALA RRFQKIDINE PSVAETTKIL
MGLKSKYEEH HGVRYTQAAL ACAAELSAKH INDRHLPDKA IDVIDEAGAR MAMQPASKRR
KTIGQAEIEA IIAKIARIPE KSVSTSDKDM LKNLERNLKM VVFGQDKAIE SLSAAIRLSR
SGLGADNKPV GSFLFAGPTG VGKTEVTNQL AKCLGLKLVR FDMSEYMEAH TVSRLIGAPP
GYVGYDQGGL LTDAVIKQPH CVVLLDEIEK AHPDVYNLLL QVMDHGTLTD NNGRKADFRH
VTLVMTTNAG VQETVRKSIG FKQQDHSHDA MSEINRVFSP EFRNRLDSII WFNHLDLTII
AKVVDKFLTE LQAQLDAKRV TLMVSDEART LLAEKGYDKA MGARPMARVV KDLIKRPLAD
EILFGELEHG GMAHVDAKDG EIVISAERLE KVT
//