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Database: UniProt
Entry: C4XFQ8_MYCFP
LinkDB: C4XFQ8_MYCFP
Original site: C4XFQ8_MYCFP 
ID   C4XFQ8_MYCFP            Unreviewed;       741 AA.
AC   C4XFQ8;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:BAH69980.1};
GN   OrderedLocusNames=MBIO_0715 {ECO:0000313|EMBL:BAH69980.1};
OS   Mycoplasmopsis fermentans (strain ATCC 19989 / NBRC 14854 / NCTC 10117 /
OS   PG18) (Mycoplasma fermentans).
OC   Bacteria; Mycoplasmatota; Mycoplasmoidales; Metamycoplasmataceae;
OC   Mycoplasmopsis.
OX   NCBI_TaxID=496833 {ECO:0000313|EMBL:BAH69980.1, ECO:0000313|Proteomes:UP000006810};
RN   [1] {ECO:0000313|EMBL:BAH69980.1, ECO:0000313|Proteomes:UP000006810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19989 / NBRC 14854 / NCTC 10117 / PG18
RC   {ECO:0000313|Proteomes:UP000006810};
RX   PubMed=19219498; DOI=10.1007/s00284-009-9362-6;
RA   Ishida N., Irikura D., Matsuda K., Sato S., Asano K.;
RT   "Molecular cloning and expression of a novel cholinephosphotransferase
RT   involved in glycoglycerophospholipid biosynthesis of Mycoplasma
RT   fermentans.";
RL   Curr. Microbiol. 58:535-540(2009).
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; AP009608; BAH69980.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4XFQ8; -.
DR   KEGG; mfp:MBIO_0715; -.
DR   PATRIC; fig|496833.3.peg.309; -.
DR   eggNOG; COG0542; Bacteria.
DR   HOGENOM; CLU_005070_4_0_14; -.
DR   Proteomes; UP000006810; 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; 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; 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; PF10431; ClpB_D2-small; 1.
DR   PRINTS; PR00300; CLPPROTEASEA.
DR   SMART; SM00382; AAA; 2.
DR   SMART; SM01086; ClpB_D2-small; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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:UP000006810}.
FT   DOMAIN          84..229
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          485..634
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          648..738
FT                   /note="Clp ATPase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01086"
FT   COILED          292..379
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   741 AA;  84037 MW;  224FB64F3B54BE40 CRC64;
     MIFGTLTLKV LKLWYNWFSI GGEIMDFNLD DLFGSNDNKS KKSSDPLKIY GRNLTDLAAR
     NELDPVINRD DEIRRMIRIL SRKTKNNPVL VGEPGVGKTA IVEGLARKIV EGQVPENLKG
     KDIFELDLAA LIAGASYQGQ FEKRLKDVLK RIEESNGDII VFIDEIHMLI GTGRNAEGGM
     DAANIIKPLM ARGKMHLIGA TTFDEYRKYI EKDAALERRM QRVDVLEPSI EDTITILRGI
     KDRFENYHNV KIQDDALVAA ARLSSRYISD RFLPDKAIDL VDEAAATIKT EINFQPEELE
     KAKQKMARLK MEKIAISSED KKKHAVRLKE IDAEIKDIEK TIKQLEDKWN FEKQRLEELS
     NLKSKLDDAR HRLNIYQKET DYEKASKILY DEIPSIKKQI EETEKEIAES GNTIVKDSVT
     SEEIANIVSK WTKIPISKLL ESDKEKLLNL ENDLKKRIKG QDAAIRLVAQ AVLRAKANIN
     DPNRPLASFL FTGPTGVGKT ELARALAYSL FDSEKQMIRL DMSEYMEKHS VSKIIGAPPG
     YVGYDSGGSL TEKIRKNPYT ILLFDEIEKA DRDVLNILLQ MMDNGAITDS KGRVINCRNL
     IIIMTSNLGS QEILKHLDQM PSIKAELLKF LSPEFVNRID EIVKFNPLTK DVINEIVELE
     LQKLATRMKD VKDVKISFTS KTVDFVGSSS YDENFGARPI KRFIQNKIES LLAYKIIDGT
     IRSGKAYKID VFAGNFVVKE A
//
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