ID U7NJI4_9GAMM Unreviewed; 982 AA.
AC U7NJI4;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 54.
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=Q671_10960 {ECO:0000313|EMBL:ERS83498.1};
OS Halomonas sp. PBN3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1397528 {ECO:0000313|EMBL:ERS83498.1, ECO:0000313|Proteomes:UP000017115};
RN [1] {ECO:0000313|EMBL:ERS83498.1, ECO:0000313|Proteomes:UP000017115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBN3 {ECO:0000313|EMBL:ERS83498.1,
RC ECO:0000313|Proteomes:UP000017115};
RX PubMed=24356826;
RA Overholt W.A., Green S.J., Marks K.P., Venkatraman R., Prakash O.,
RA Kostka J.E.;
RT "Draft genome sequences for oil-degrading bacterial strains from beach
RT sands impacted by the deepwater horizon oil spill.";
RL Genome Announc. 1:e01015-13(2013).
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:ERS83498.1}.
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DR EMBL; AXCA01000190; ERS83498.1; -; Genomic_DNA.
DR RefSeq; WP_023006963.1; NZ_AXCA01000190.1.
DR AlphaFoldDB; U7NJI4; -.
DR PATRIC; fig|1397528.3.peg.2768; -.
DR eggNOG; COG0553; Bacteria.
DR Proteomes; UP000017115; 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; 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};
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 163..331
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 498..663
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT MOTIF 277..280
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01821"
FT BINDING 176..183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01821"
SQ SEQUENCE 982 AA; 109580 MW; 96279DC4AD6F1FA0 CRC64;
MSDFSPGQRW ISDGEAELGL GTILSCDARS VTVLFGASQE TRTYSSRQAP LTRVAFGSGD
RIRAAEGWTL TVDDTKEVDG LIVYIGEDDQ GELRELSEAR LADSMQFDQA RDRLLTGQVN
RNDWFDLRFR TLHHYHRVEQ NPALGLAGPR IDLIPHQLYI ADEVARRHAP RVLLADEVGL
GKTIEAGLIL HRLLLTGRAE RALILVPASL THQWLVELLR RFALEVTLLD EQQSQAHGEG
NPFEAGQLIL ASQDWLFANP HRQAQAAACD WDLLIVDEAH HLDWSEEQVG PGYACVERLA
ADSEGVLLLT ATPEQMGVES HFARLRLLDP DRYHSLEAFR EEEAHYVEVA EAIDALERLP
GDDADRARVA AVIDEPDSLA LLDTLADPER GDDQHAAARD QLRDQLLDRH GTGRVMFRNS
RRHVGGFPER RLHVTELEPP SAYRRVLRKL SRDEDYLDEL LIETGLDHPE VLVYLDAMYR
ALADDPLNGE PWWQIDPRVN WLLERLADDG EAGLAGDKVL VIAHDAETAQ GLAEALRVLG
GYHAPVFHEG LSLVERDRAA AAFADEEEGC QVLVCSEIGS EGRNFQFCRH LVMFDLPLHP
DQLEQRIGRL DRIGQRHAIE LHVPVFAGSP GEKLLRWYRD GMDAFSAPHG IGSEIHDAFG
DALADALLDD EALDEVVEET RALFESRLAE RDAGRNRLLE LNACRHERAE AVAAAIGELD
EDRALPRYLD LALDIFGVDS QELGGGIQHL VAGPQMLDGL PGLAKGEEGF SATFSRRRAL
ARDDVQRLSW EHPMVREMMG RILDGSMGNT ALALLKHPAL PAGRVMVELI YRTHCPAPRK
LHLNRFLPPT AVRVLLDESG ANLTDKISFT GLSKNLQKVK KAMARDLIRS RLEVLRELLD
RGEGEAEREL PSIVEAAQVR MRDELDGELS RLTALARRNP AVREAELTAL REERDNLDAA
IEGARLRLDA VRVIVTVGEE SR
//
