ID M1PCU1_BARAA Unreviewed; 783 AA.
AC M1PCU1;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE SubName: Full=Endopeptidase Clp ATP-binding chain a {ECO:0000313|EMBL:AGF74416.1};
GN Name=clpA {ECO:0000313|EMBL:AGF74416.1};
GN OrderedLocusNames=BAnh1_05370 {ECO:0000313|EMBL:AGF74416.1};
OS Bartonella australis (strain Aust/NH1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=1094489 {ECO:0000313|EMBL:AGF74416.1, ECO:0000313|Proteomes:UP000011729};
RN [1] {ECO:0000313|EMBL:AGF74416.1, ECO:0000313|Proteomes:UP000011729}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Aust/NH1 {ECO:0000313|EMBL:AGF74416.1,
RC ECO:0000313|Proteomes:UP000011729};
RX PubMed=23555299; DOI=10.1371/journal.pgen.1003393;
RA Guy L., Nystedt B., Toft C., Zaremba-Niedzwiedzka K., Berglund E.C.,
RA Granberg F., Naslund K., Eriksson A.S., Andersson S.G.;
RT "A gene transfer agent and a dynamic repertoire of secretion systems hold
RT the keys to the explosive radiation of the emerging pathogen Bartonella.";
RL PLoS Genet. 9:E1003393-E1003393(2013).
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003123; AGF74416.1; -; Genomic_DNA.
DR RefSeq; WP_015397924.1; NC_020300.1.
DR AlphaFoldDB; M1PCU1; -.
DR STRING; 1094489.BAnh1_05370; -.
DR KEGG; baus:BAnh1_05370; -.
DR PATRIC; fig|1094489.3.peg.660; -.
DR eggNOG; COG0542; Bacteria.
DR HOGENOM; CLU_005070_4_1_5; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000011729; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0043335; P:protein unfolding; IEA:InterPro.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
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 764..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 783 AA; 87085 MW; 54AB3957B84005ED CRC64;
MPSFTPSLEE VLQRALTIAT QAQHEYATLE HLLLALLDDA DASSVIRACK VDLEELRERL
THYIQSELDI QIRTDEDTKP TAFFQRVIQR AVIHAQSVGK DEVSGANVLV AIFSERESYA
AYFLQEMGMT RYDAVRFISH GIMHDDGLSL LLEDLEEQLE QQVFDRGEKV ASALSVYCVD
LNRKARSGKI DLLIGRDVEI SRMIQILCRR SKNNPLLVGD PGVGKTAIIE GLARRIIDGQ
VPEVLSNTTI FALDMGGLVA GTRYRGDFEE RLKQIIKEFA QHPGAVLFID EIHTLIGAGA
TSGGNMDAAN LLKPVLSSGV IRCIGSTTYR EYRKIFEQDR ALERRFQKVD VNEPSIADAI
KILQGLKPYF EDFHQLKYTD EAVKASVELS SRYMADRRLP DKAIDVVDES GAAQMLLPKK
RRKKSIGVKE IEATIATMAR IPSKTISGDD QKLLCNLEKE LKQVVYGQDQ AITALVSSIK
LARAGLREAE KPIGSYLFSG PTGVGKTEIA RQLASSLGIG LLRFDMSEYM EQHTVARLIG
APPGYVGFDQ GGLLTDAVDQ KPHAVVLLDE IEKAHPELFN ILLQVMDYGK LTDHNGKKID
FRNVILIMTT NAGASDMAKS AIGFGKVLRD SDDVEAINRL FTPEFRNRLD AIIRFAPLSR
LMISRVVQKF IFQLEAQLID QEITFDVSVS AMAWLANKGY DVQMGARPLG YVIQEYIKKP
LADEILFGKL RNGGTVRVST HKLNEGKETL KLQISPSNIP IHSKNRKAES SVKKRIAKKN
SAT
//