ID W2D6K7_9PSED Unreviewed; 948 AA.
AC W2D6K7;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=H096_29473 {ECO:0000313|EMBL:ETK15024.1};
OS Pseudomonas sp. FH1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1284392 {ECO:0000313|EMBL:ETK15024.1, ECO:0000313|Proteomes:UP000018863};
RN [1] {ECO:0000313|EMBL:ETK15024.1, ECO:0000313|Proteomes:UP000018863}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FH1 {ECO:0000313|EMBL:ETK15024.1,
RC ECO:0000313|Proteomes:UP000018863};
RX PubMed=24286439; DOI=10.1111/1462-2920.12345;
RA Rhodes G., Bosma H., Studholme D., Arnold D.L., Jackson R.W., Pickup R.W.;
RT "The rulB gene of plasmid pWW0 is a hotspot for the site-specific insertion
RT of integron-like elements found in the chromosomes of environmental
RT Pseudomonas fluorescens group bacteria.";
RL Environ. Microbiol. 16:2374-2388(2014).
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:ETK15024.1}.
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DR EMBL; AOHM01000129; ETK15024.1; -; Genomic_DNA.
DR RefSeq; WP_033902734.1; NZ_AOHM01000129.1.
DR AlphaFoldDB; W2D6K7; -.
DR PATRIC; fig|1284392.3.peg.5730; -.
DR Proteomes; UP000018863; 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; 106594 MW; E3676C4B5A7877BB CRC64;
MAQQYQPGQR WISDSEAELG LGTVLAQDGR LLTVLYPATG DTRQYALRNA PLTRVRFSPG
DSITHFEGWK MTVQEVDDVD GLLVYHGLNG QNEQVTLPET QLSNFIQFRL ASDRLFAGQI
DPLAWFSLRY HTLEHTSRQL QSSLWGLGGV RAQPIAHQLH IAREVADRIA PRVLLADEVG
LGKTIEAGLV IHRQLLSGRA NRVLILVPEN LQHQWLVEMR RRFNLQVALF DEERFIESDA
TNPFEDTQLA LVALEWLVDD EKAQDALFAA GWDLLVVDEA HHLVWHEEKA SPEYALVEQL
AEVIPGVLLL TATPEQLGQD SHFARLRLLD PNRFHDLAAF RAESENYRPV AEAVQELLDK
GRLSPAAHKT IQGFLGDEGE ALLTAVNDGD TEASARLVRE LLDRHGTGRV LFRNTRAAVQ
GFPERKLHAY PLPNPDEYLE LPLGEHAELY PEVSFQSQPD IEEENRWWRF DPRVEWLIDQ
LKMLKRTKVL VICAHAETAM DLEDALRVRS GIPATVFHEG MNILERDRAA AYFADEEFGA
QVLICSEIGS EGRNFQFSHH LVLFDLPSHP DLLEQRIGRL DRIGQKHVIE LHVPYLETSP
QERLFQWYHE ALNAFLNTCP TGNALQHQFG PRLLPLLENA DDGEWQALID EARAERERLE
EELHTGRDRL LELNSGGAGE GDALVEDILE QDDQFALPIY METLFDAFGI DSEDHSENAL
ILKPSEKMLD ASFPLGDDEG VTITYDRNQA LSREDMQFIT WEHPMVQGGM DLVLSGSMGN
TAVALIKNKA LKPGTVLLEL LYVSEVVAPR SLQLGRYLPP AALRCLLDAN GNDLSSRVSF
VTLNDQLESV PRASANKFIQ AQRDQLTPRI NAGEEKITPQ HAERVAEAKR RLAADTDEEL
ARLTALQAVN PTVRDSELVA LRAQREQGLA MLDKAALRLE AIRVLVAG
//
