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Database: UniProt
Entry: Q8G3K5_BIFLO
LinkDB: Q8G3K5_BIFLO
Original site: Q8G3K5_BIFLO 
ID   Q8G3K5_BIFLO            Unreviewed;      1712 AA.
AC   Q8G3K5;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=Activase {ECO:0008006|Google:ProtNLM};
GN   OrderedLocusNames=BL1754 {ECO:0000313|EMBL:AAN25537.1};
OS   Bifidobacterium longum (strain NCC 2705).
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=206672 {ECO:0000313|EMBL:AAN25537.1, ECO:0000313|Proteomes:UP000000439};
RN   [1] {ECO:0000313|EMBL:AAN25537.1, ECO:0000313|Proteomes:UP000000439}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCC 2705 {ECO:0000313|Proteomes:UP000000439};
RX   PubMed=12381787; DOI=10.1073/pnas.212527599;
RA   Schell M.A., Karmirantzou M., Snel B., Vilanova D., Berger B., Pessi G.,
RA   Zwahlen M.C., Desiere F., Bork P., Delley M., Pridmore R.D., Arigoni F.;
RT   "The genome sequence of Bifidobacterium longum reflects its adaptation to
RT   the human gastrointestinal tract.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14422-14427(2002).
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR   EMBL; AE014295; AAN25537.1; -; Genomic_DNA.
DR   RefSeq; NP_696901.1; NC_004307.2.
DR   RefSeq; WP_011068820.1; NC_004307.2.
DR   STRING; 206672.BL1754; -.
DR   EnsemblBacteria; AAN25537; AAN25537; BL1754.
DR   KEGG; blo:BL1754; -.
DR   PATRIC; fig|206672.9.peg.1809; -.
DR   HOGENOM; CLU_002393_1_0_11; -.
DR   OrthoDB; 9177882at2; -.
DR   PhylomeDB; Q8G3K5; -.
DR   Proteomes; UP000000439; Chromosome.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.420.40; -; 4.
DR   InterPro; IPR002731; ATPase_BadF.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018709; CoA_activase_DUF2229.
DR   InterPro; IPR008275; CoA_E_activase_dom.
DR   NCBIfam; TIGR00241; CoA_E_activ; 1.
DR   PANTHER; PTHR32329:SF4; ACTIVATOR OF 2-HYDROXYACYL-COA DEHYDRATASE-RELATED; 1.
DR   PANTHER; PTHR32329; BIFUNCTIONAL PROTEIN [INCLUDES 2-HYDROXYACYL-COA DEHYDRATASE (N-TER) AND ITS ACTIVATOR DOMAIN (C_TERM)-RELATED; 1.
DR   Pfam; PF01869; BcrAD_BadFG; 2.
DR   Pfam; PF09989; DUF2229; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE   4: Predicted;
KW   Iron {ECO:0000256|ARBA:ARBA00023014};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00023014};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000439}.
FT   DOMAIN          21..279
FT                   /note="ATPase BadF/BadG/BcrA/BcrD type"
FT                   /evidence="ECO:0000259|Pfam:PF01869"
FT   DOMAIN          351..605
FT                   /note="ATPase BadF/BadG/BcrA/BcrD type"
FT                   /evidence="ECO:0000259|Pfam:PF01869"
FT   DOMAIN          746..964
FT                   /note="DUF2229"
FT                   /evidence="ECO:0000259|Pfam:PF09989"
FT   REGION          1101..1138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1173..1208
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1244..1267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1247..1267
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1712 AA;  186030 MW;  4C255B692D5A8C82 CRC64;
     MVDIATDASL KPASHPKPLR VGLDIGSTTV KAVVLDQSDS LGDTLFSDYR RHHANVRATV
     AGLLVDIHKK LVDLGRGDEP IRLSITGSGG LALADNLHVP FIQEVIAETE AIDKEYPQAD
     VIIELGGEDA KITYLKPTPE QRMNGSCAGG TGAFIDQMST LLDTDAAGLN EMAKSYENLY
     PIASRCGVFA KTDLQPLIND GAAKPDLAAS IFTAVATQTI AGLASGRPIH GTVIFLGGPL
     FFMSELRAAF QRALEGKVDE FIVPTDAHLY VAYGSALQAD TDSDDQGHHF EAYTCDEILK
     RLDELKNLPS NTPTMPPLFP TEADREDFNK RHHKEHIHIG TLEGAHGPHF LGIDAGSTTI
     KATLVNDDRE IVWSSYANNE GSPLTAAINI VKKIQSELPE GAWIARSCAT GYGEGLITTG
     LHLDEGVVET MAHYRGAEMV SPGVTAVIDI GGQDMKYLAI TDGVIDSIAV NEACSSGCGS
     FLQTFAMSMG LTIQEFTQKA LASTHPVDLG SRCTVFMNSS VKQAQKEGAS IEDIAAGLCY
     SVVRNALYKV IKLRDSGELG DTVVVQGGTF LNDAVLRAFE LLTEREVTRP NIAGLMGAFG
     AALTARMHYE DIADDDNAHV GADGRSVDAA AAEESAAGDE PNAAAHAGEI VVDGVRHTVS
     SILTGEALNE MSMTTERDVC KLCQNHCKLT ITTFSDGSRF VTGNRCERGG DAKKKRSDRP
     NLYDYKYKRC FAYRRLTDKN ATRGEIGIPR ALNMYENYPF WFTLLTSLGF KVMISGRSSH
     ELFETGIESI ASENICYPAK LVHGHIKWLL NKGMKTIFYP CVSYEDNLVP NTDNHYNCPV
     VANYPLVVGA NMPELRDPDV RYMHPYFNLA NHELMVDRIV EEFAWASVSR EEAETAVKAA
     YAEDKVFKHD VQQEGLKALA YMKEHDCRGI VLAGRPYHID PEINHGIPET ICALGMVVLS
     EDSICELQPG EKLDLTDFLS EGEEDPRKKN ANGFRHVDDR KVTVNRMPLR VTNQWAYHSR
     LYAAAHFVAS YPGLELVQLN SFGCGLDAIT TDQVAEILAD KADVYTLLKI DEVSNLGAAK
     IRLRSLKAAV EEREANKARM AKAALATSDE SGSAESDAPR NAAHAAAQAA ARKAQEQAES
     DLATAQAALA EAQAAVAAAE AKVKAADRPV DAADAGSDAA APANAPKSTG FRKTGSKAPT
     PGRQVLLDAT MAANPKLTKA MRDASKRAAK RDIADVRLAA LGDGTTNDAA NAKSKSAKSK
     SGHNNATMSR YAHREKFVKD MKKDYTIVAP QMSPIHFSLV ESVIRSGGYK FDILKHASRE
     DVETGLKYVN NDACYPAIMV IGQLIDAILE GKYDPDKVCL AITQTGGMCR ATNYFGLIRK
     ALIDAGYPQI PVIAISTQGL EDNPGFKVTP ALLHRTVKAL ILGDLLMKCL YRVRPYEVEK
     GAANRLYEQW DVIVREALEH HGFSKTAAKT PWLKRRYLPY PVLAREIVKS FDALPLKDVP
     RKVRVGVVGE ILVKYQPDAN NHVVDVIESQ DCEAVVPGIM EFMTTRPYIT DWNEKYLGTG
     GNKTLYALMR WSLDRYNAPI KAAIATSHGK FKQDDPMPEL VEKAAEVTSI GVQAGEGWLL
     TAEILELIEQ GCPNVICAQP FACLPNHVTG RGMFGKIRRL HPEANIVSID YDPGASEANQ
     LNRIKLMIAA AKKAHNAKFA EAGEPQGFTS AD
//
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