ID F2RCG0_STRVP Unreviewed; 656 AA.
AC F2RCG0;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Putative CbxX or CfqX family protein {ECO:0000313|EMBL:CCA54318.1};
GN OrderedLocusNames=SVEN_1031 {ECO:0000313|EMBL:CCA54318.1};
OS Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS 4526 / NBRC 13096 / PD 04745).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=953739 {ECO:0000313|EMBL:CCA54318.1, ECO:0000313|Proteomes:UP000006854};
RN [1] {ECO:0000313|EMBL:CCA54318.1, ECO:0000313|Proteomes:UP000006854}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 /
RC PD 04745 {ECO:0000313|Proteomes:UP000006854};
RX PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA Pullan S.T., Bibb M.J., Merrick M.;
RT "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT provides new insights into global nitrogen regulation in actinomycetes.";
RL BMC Genomics 12:175-175(2011).
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the CbxX/CfxQ family.
CC {ECO:0000256|ARBA:ARBA00010378}.
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DR EMBL; FR845719; CCA54318.1; -; Genomic_DNA.
DR AlphaFoldDB; F2RCG0; -.
DR STRING; 953739.SVEN_1031; -.
DR KEGG; sve:SVEN_1031; -.
DR PATRIC; fig|953739.5.peg.3099; -.
DR eggNOG; COG0464; Bacteria.
DR HOGENOM; CLU_008749_5_1_11; -.
DR Proteomes; UP000006854; Chromosome.
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 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.
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:UP000006854}.
FT DOMAIN 405..546
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 297..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..356
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 656 AA; 71184 MW; D5718DCB4684417A CRC64;
MRSNPVHAKT VVGDPMDIGT QGAQAPAELA WLRGVDAYTM GAYPQAEDEF RTAVRIDPGM
ADAWLGLHAL RVDTTTALLR MYRNRDRFGE QRARYRRTLN SWYWLGWWVQ PVLESPRDLL
LAHASHWLDG RHVPELDRAL AGLPPVDTDP QVRFLHACRA YLVKDWDQLV RHTDSLVDDP
LLGIEAGLFG GMARVRLEMY GQAEPLLSAS LMRCRSEQPQ RKELRYWLAR AHEGTGRSAA
ALPLYRAVHR IDPTFMDTAA RLAAIAEYDG FEGYDGVDDP AGLATVALGT LGGGLGQDGV
DTAPGADPEG GGPVGDGLRL APEPAPPVAP AASPEPVRQK APLPAQPVPP RFPAGPTDPV
LLAEALAELE GMVGLEPVKR QVKALSAQLE MARLRAGQGL PVQPPKRHFV FSGPSGTGKT
TVARILGRVF YALGLLGGDH LVEAQRADLV GEFLGQTAVK ANELIDSAVG GVLFVDEAYA
LSNTGYSKGD AYGDEALQVL LKRAEDNRDH LVVILAGYPE GMDRLLSTNP GLSSRFTTRV
DFPSYRPLEL TAIGEVLAAA NGDGWDEEAV EELRSISGHV VEQGWIDELG NGRFLRTLYE
KSCAYRDLRL SGYASTPTRE DLATLRLADL MQAYGEVLSG RGPVDRGPQQ EPPPGY
//