ID A0A0C1XFI5_9ACTN Unreviewed; 645 AA.
AC A0A0C1XFI5;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=CbxX/CfqX {ECO:0000313|EMBL:KIF73493.1};
GN ORFNames=QR77_04975 {ECO:0000313|EMBL:KIF73493.1};
OS Streptomyces sp. 150FB.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1576605 {ECO:0000313|EMBL:KIF73493.1, ECO:0000313|Proteomes:UP000031584};
RN [1] {ECO:0000313|EMBL:KIF73493.1, ECO:0000313|Proteomes:UP000031584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=150FB {ECO:0000313|EMBL:KIF73493.1,
RC ECO:0000313|Proteomes:UP000031584};
RA Tarkka M.T., Feldhahn L., Kruger D., Buscot F., Wubet T.;
RT "Genome sequence of the mycoparasite antagonist Streptomyces sp. strain FB
RT 150.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the CbxX/CfxQ family.
CC {ECO:0000256|ARBA:ARBA00010378}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIF73493.1}.
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DR EMBL; JTHL01000001; KIF73493.1; -; Genomic_DNA.
DR RefSeq; WP_040019858.1; NZ_JTHL01000001.1.
DR AlphaFoldDB; A0A0C1XFI5; -.
DR STRING; 1576605.QR77_04975; -.
DR OrthoDB; 9806903at2; -.
DR Proteomes; UP000031584; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041627; AAA_lid_6.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR000641; CbxX/CfxQ.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR049078; T7SS_EccA1-like_N.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR43392; AAA-TYPE ATPASE FAMILY PROTEIN / ANKYRIN REPEAT FAMILY PROTEIN; 1.
DR PANTHER; PTHR43392:SF2; AAA-TYPE ATPASE FAMILY PROTEIN _ ANKYRIN REPEAT FAMILY PROTEIN; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17866; AAA_lid_6; 1.
DR Pfam; PF21545; T7SS_EccA1_N; 1.
DR PRINTS; PR00819; CBXCFQXSUPER.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
DR PROSITE; PS50005; TPR; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000031584};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT REPEAT 12..45
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 397..538
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 276..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..348
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 645 AA; 70214 MW; F7D507D985B8B24C CRC64;
MDSGTQGTGA PADLAWVRGM DAYTMGAYPQ AEDEFRTAVR LDPGMADGWL GLHALRVETT
TALLRMYSHH ARFGEQRARH GRTLNSWYWL GWWVQPVLES GRDLLLAHAS HWLDGRHVPE
LDRALAGLPP VDADPQVRFL HACRSYLVKD WDQLVRHTER LVDDPLLGIE AGLFGGMARV
RLEMYGQAEP LLSAALMRCR SEQPQRKELR YWLARAREGT GRSAAALPLY RAVHRIDPAF
MDTAARLAAI TDSDGYDNSD DPAGLASVAL AGFGQDAADA QSEADTAYGQ EPHFGSEPPS
APSQSSPSSQ SSSQLPGAIP PAVQPDDVRE KAPPPPVGPP PPQFPDGPTD PVLLAQALAE
LERMVGLEPV KRQVKALSAQ LNMARLRARE GLPLQPPKRH FVFSGPSGTG KTTVARILGR
IFYALGLLGG DHLVEAQRAD LVGEFLGQTA VKANELIDSA IGGVLFVDEA YSLSNSGYTK
GDAYGDEALQ VLLKRAEDSR DHLVVILAGY PEGMDRLLAT NPGLSSRFTS RVDFPSYRPL
ELTAIGEVLA AENGDLWDEE SRDELRSISA HVVDQGWIDE LGNGRFLRTL YEKSCAYRDL
RLSGYSSTPG RDDLATLRLP DLMQAYGEVL SGRGPVNRGP QDPAG
//
