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Database: UniProt
Entry: F4KUD4_HALH1
LinkDB: F4KUD4_HALH1
Original site: F4KUD4_HALH1 
ID   F4KUD4_HALH1            Unreviewed;       898 AA.
AC   F4KUD4;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 67.
DE   SubName: Full=ATPase AAA-2 domain protein {ECO:0000313|EMBL:AEE51216.1};
GN   OrderedLocusNames=Halhy_3358 {ECO:0000313|EMBL:AEE51216.1};
OS   Haliscomenobacter hydrossis (strain ATCC 27775 / DSM 1100 / LMG 10767 / O).
OC   Bacteria; Bacteroidota; Saprospiria; Saprospirales; Haliscomenobacteraceae;
OC   Haliscomenobacter.
OX   NCBI_TaxID=760192 {ECO:0000313|EMBL:AEE51216.1, ECO:0000313|Proteomes:UP000008461};
RN   [1] {ECO:0000313|EMBL:AEE51216.1, ECO:0000313|Proteomes:UP000008461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27775 / DSM 1100 / LMG 10767 / O
RC   {ECO:0000313|Proteomes:UP000008461};
RX   PubMed=21886862; DOI=10.4056/sigs.1964579;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Daligault H., Lapidus A., Zeytun A., Nolan M., Lucas S., Del Rio T.G.,
RA   Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA   Pagani I., Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., Pati A.,
RA   Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Rohde M.,
RA   Verbarg S., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Woyke T.;
RT   "Complete genome sequence of Haliscomenobacter hydrossis type strain (O).";
RL   Stand. Genomic Sci. 4:352-360(2011).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 1100;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Pagani I.,
RA   Daligault H., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Verbarg S., Frueling A.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "Complete sequence of chromosome of Haliscomenobacter hydrossis DSM 1100.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC       {ECO:0000256|ARBA:ARBA00026057}.
CC   -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC       {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
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DR   EMBL; CP002691; AEE51216.1; -; Genomic_DNA.
DR   AlphaFoldDB; F4KUD4; -.
DR   STRING; 760192.Halhy_3358; -.
DR   KEGG; hhy:Halhy_3358; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_2_10; -.
DR   OrthoDB; 9803641at2; -.
DR   Proteomes; UP000008461; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
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; 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   PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR   PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 78, MITOCHONDRIAL; 1.
DR   Pfam; PF00004; AAA; 1.
DR   Pfam; PF07724; AAA_2; 1.
DR   Pfam; PF17871; AAA_lid_9; 1.
DR   Pfam; PF02861; Clp_N; 2.
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   Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|SAM:Coils};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU004432};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008461};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW   ProRule:PRU01251}.
FT   DOMAIN          3..145
FT                   /note="Clp R"
FT                   /evidence="ECO:0000259|PROSITE:PS51903"
FT   REGION          867..898
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          397..488
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   898 AA;  100881 MW;  649EE2C9966A48AD CRC64;
     MTYDNFTIKA QESILKSQQI AAGLDQQQVD TVHLIKGILE TDESVAGFLL GKSEVNLDML
     RRKLDEAILK YPKVQGSDKQ FLTTDANKSL SRAKVLLKEF GDQYISVELM LLGIVQGDDS
     GAKLLKELGA NEQLLKGAIN ELRKGRKVTD QNSEDSYNAL AKYAINLNER AESGKLDPIV
     GRDDEIRRVL HILSRRKKNN PILIGEAGVG KTAIVEGLAW RIVKGDVPES LQSKKIFVLD
     IAALIAGAKY KGEFEERLKG VIQEVTESND TIILFVDEIH TLIGAGGGNG AMDAANILKP
     ALARGELRTI GATTLDEYQK YFEKDKALVR RFQEVLIDEP SVEDTISILR GLQERYEVYH
     KIEIMDEALV AAAELSSRYI SDRQLPDKAI DLIDEAAARL RLELDSLPEE IDEWDRKVRQ
     LEIEREAVKR EKNKKQQDLI EENIANAKQK RDSLMAAWKG EKELVDTVQG VKKKMEELEI
     QAERAERASD YEMVAKIRYG ELEDQKQILK VAEEKLAALP EDSRFTNDKV TANDIAYIVS
     RWTGIPIDKM TQSEKDKLLS LEKEIGQRLI GQDEAVKAVS DAIRRSRAGL QDADRPIGSF
     IFLGPTGVGK TELAKTIAEV LFDDEKAMTR IDMSEYQEKH TVSRLVGAPP GYVGYDEGGQ
     LTEAVRRRPY SIILLDEIEK AHPDTFNILL QVLDDGRLTD NKGRVANFKN TIIIMTSNMG
     SDLIMENFDD LEEMGEKHRT EIIATTKEEV FNLLKENLRP EFLNRIDEQI LFLPLNKSEI
     KQILDLLLKK TQKMLAKQGI ILKVSDPAKD LLADMGYDPQ FGARPMKRVL QKDVINELSK
     LVLSGEVALG DTIYVHTDKK GLTFSKEPYE GAINLPPDPV DDGDDDEKEV EKPVEEKA
//
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