ID J2RGX4_9PSED Unreviewed; 948 AA.
AC J2RGX4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=RNA polymerase-associated protein RapA {ECO:0000256|HAMAP-Rule:MF_01821};
DE EC=3.6.4.- {ECO:0000256|HAMAP-Rule:MF_01821};
DE AltName: Full=ATP-dependent helicase HepA {ECO:0000256|HAMAP-Rule:MF_01821};
GN Name=rapA {ECO:0000256|HAMAP-Rule:MF_01821};
GN ORFNames=PMI28_05614 {ECO:0000313|EMBL:EJM48404.1};
OS Pseudomonas sp. GM48.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144330 {ECO:0000313|EMBL:EJM48404.1, ECO:0000313|Proteomes:UP000007293};
RN [1] {ECO:0000313|EMBL:EJM48404.1, ECO:0000313|Proteomes:UP000007293}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM48 {ECO:0000313|EMBL:EJM48404.1,
RC ECO:0000313|Proteomes:UP000007293};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
CC -!- FUNCTION: Transcription regulator that activates transcription by
CC stimulating RNA polymerase (RNAP) recycling in case of stress
CC conditions such as supercoiled DNA or high salt concentrations.
CC Probably acts by releasing the RNAP, when it is trapped or immobilized
CC on tightly supercoiled DNA. Does not activate transcription on linear
CC DNA. Probably not involved in DNA repair. {ECO:0000256|HAMAP-
CC Rule:MF_01821}.
CC -!- SUBUNIT: Interacts with the RNAP. Has a higher affinity for the core
CC RNAP than for the holoenzyme. Its ATPase activity is stimulated by
CC binding to RNAP. {ECO:0000256|HAMAP-Rule:MF_01821}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RapA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01821}.
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:EJM48404.1}.
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DR EMBL; AKJM01000180; EJM48404.1; -; Genomic_DNA.
DR RefSeq; WP_007992421.1; NZ_AKJM01000180.1.
DR AlphaFoldDB; J2RGX4; -.
DR PATRIC; fig|1144330.3.peg.5464; -.
DR OrthoDB; 9814088at2; -.
DR Proteomes; UP000007293; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016817; F:hydrolase activity, acting on acid anhydrides; IEA:InterPro.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:UniProtKB-UniRule.
DR CDD; cd18011; DEXDc_RapA; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 2.30.30.140; -; 1.
DR Gene3D; 2.30.30.930; -; 1.
DR Gene3D; 3.30.360.80; -; 1.
DR Gene3D; 6.10.140.1500; -; 1.
DR Gene3D; 6.10.140.2230; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR HAMAP; MF_01821; Helicase_RapA; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR023949; Helicase_RapA.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR022737; RapA_C.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR InterPro; IPR040765; Tudor_1_RapA.
DR InterPro; IPR040766; Tudor_2_RapA.
DR PANTHER; PTHR45766; DNA ANNEALING HELICASE AND ENDONUCLEASE ZRANB3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45766:SF3; SWI_SNF-RELATED MATRIX-ASSOCIATED ACTIN-DEPENDENT REGULATOR OF CHROMATIN SUBFAMILY A-LIKE PROTEIN 1; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF12137; RapA_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR Pfam; PF18339; Tudor_1_RapA; 1.
DR Pfam; PF18337; Tudor_RapA; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 3: Inferred from homology;
KW Activator {ECO:0000256|ARBA:ARBA00023159, ECO:0000256|HAMAP-Rule:MF_01821};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01821}; Coiled coil {ECO:0000256|SAM:Coils};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW Rule:MF_01821};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|HAMAP-Rule:MF_01821};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01821};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01821};
KW Transcription {ECO:0000256|ARBA:ARBA00023163, ECO:0000256|HAMAP-
KW Rule:MF_01821};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015, ECO:0000256|HAMAP-
KW Rule:MF_01821}.
FT DOMAIN 164..332
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 473..627
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 642..669
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 278..281
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01821"
FT BINDING 177..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01821"
SQ SEQUENCE 948 AA; 106711 MW; A49B7747AB6FB29F CRC64;
MAQQYQPGQR WISDSEAELG LGTVLAQDGR LLTVLYPATG DTRQYALRNA PLTRVRFSPG
DTITHFEGWK LTVREVDDID GLLVYHGLNG QSEVVTLPET QLSNFIQFRL ASDRLFAGQI
DPLAWFSLRY HTLEHTSRQL QSSLWGLGGV RAQPIAHQLH IAREVADRIA PRVLLADEVG
LGKTIEAGLV IHRQLLSGRA SRVLILVPEN LQHQWLVEMR RRFNLQVALF DEERFIESDA
SNPFEDTQLA LVALEWLVDD EKAQDALFAA GWDLMVVDEA HHLVWHEDQV SPEYSLVEQL
AETIPGVLLL TATPEQLGQD SHFARLRLLD PNRFHDLQAF RAESENYRPV AEAVQELLDQ
GRLSPQAHKT IHGFLGNEGE ALLAAVNDGD TEASARLVRE LLDRHGTGRV LFRNTRAAVQ
GFPERKLHPY PLPCPDEYLE LPLGDHAELY PEVSFQAQPD ASEEDRWWKF DPRVEWLIDQ
LKMLKRTKVL VICAHAETAM DLEDALRVRS GIPATVFHEG MNILERDRAA AYFADEEFGA
QVLICSEIGS EGRNFQFSHH LVLFDLPSHP DLLEQRIGRL DRIGQKHIIE LHVPYLETSP
QERLFQWYHE ALNAFLNTCP TGNALQHQFG PRLLPLLEEA DDSEWQALID EARTERERLE
AELHTGRDRL LELNSGGAGE GDALVEDILE QDDQFALPIY METLFDAFGI DSEDHSENAL
ILKPSEKMLD ASFPLGDDEG VTITYDRNQA LSREDMQFIT WEHPMVQGGM DLVLSGSMGN
TAVALIKNKA LKPGTVLLEL LYVSEVVAPR SLQLGRYLPP AALRCLLDTN GNDLSSRVSF
ETLNDQLESV PRASANKFIQ AQRDQLTPRI NAGEAKILPR HTERVAEAQR RLAADTEEEL
ARLTALQAVN PTVRDSELVA LRNQREQGLA MLDKAALRLE AIRVLVAG
//
