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Database: UniProt
Entry: A1S7A5_SHEAM
LinkDB: A1S7A5_SHEAM
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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
//
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