ID A0A1S6HXW4_9GAMM Unreviewed; 968 AA.
AC A0A1S6HXW4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=Sps_05282 {ECO:0000313|EMBL:AQS40351.1};
OS Shewanella psychrophila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=225848 {ECO:0000313|EMBL:AQS40351.1, ECO:0000313|Proteomes:UP000189545};
RN [1] {ECO:0000313|EMBL:AQS40351.1, ECO:0000313|Proteomes:UP000189545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP2 {ECO:0000313|EMBL:AQS40351.1,
RC ECO:0000313|Proteomes:UP000189545};
RA Xu G., Jian H.;
RT "Complete genome sequence of Shewanella psychrophila WP2, a deep sea
RT bacterium isolated from west Pacific sediment.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP014782; AQS40351.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S6HXW4; -.
DR STRING; 225848.Sps_05282; -.
DR KEGG; spsw:Sps_05282; -.
DR OrthoDB; 9814088at2; -.
DR Proteomes; UP000189545; Chromosome.
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};
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..332
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 491..678
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT MOTIF 278..281
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 968 AA; 109036 MW; CE1F25BCAB60A342 CRC64;
MPFSLGQRWI SDTESELGLG TVVGLEGRMV TLMFPATDEN RLFSRTEAPL TRVIYNPGDK
VESHEGWSLT VSELEEKNEL IIYHGIHTET GEQVSLRETL LNHNVRFNKP QDRLFAGQID
RLDRFGVRYQ SQLLRNKLAT SDLLGLQGPR VGLIPHQQWI AHEVGRRFAP RVLLADEVGL
GKTIEAGLII HQQLLTGRAE RILVIVPDTL RHQWLVEMLR RFNLKFSVFD EDRCIEAYAD
NDNPFYTEQL VICSLELLRK KKRLEQAIDA DWDLMIVDEA HHLEWTEEAP SRAYRIVEAL
SEVVPGVLLL TATPDQLGHQ SHFARLRLLD PDRFYDYEAF LEEENSYKDV ASAAEALASG
DTLSSEAVSQ LTTLLSEKDI DETLELIQAS DADVDKQQAA RDELLQDLLD RHGTGRVLYR
NSRASVKGFP TRIFHAHPQA MPSQYVTAAR VGAMMNGHLD TPAKVKQALS PEKIYQDFES
SSASWWKFDP RVDWLIEFLK TNRSKKVLII ASQAETALSL EEALRTREGI QATVFHEGMS
IIERDKAGAY FAQETGGAQA LICSEIGSEG RNFQFASQLI LFDLPLNPDL LEQRIGRLDR
IGQNNDVEIH LPYLAGTAQE CLMQWYHTGL NAFEQTCPSG HILFNEFSES LLSQLITQDE
SALQELLSNT QTRYQELKTA MEQGRDKLLE INSHGGDRAT KLVQRLAERD EDTQLIGSVI
RLWDIIGVEQ EDCGENTIVL KTSEHMMFPT YPGLSEDGMT ITFDREMALS RDDIALITQE
HPLVQTGLDL ITSSETGSTS VAVLKNKALP AGTIFLELIY MADASAPKSS QLYRYLPPTP
VRILLDKNGN NLSDNVTYES FNKQLSAVNR HIASKLVNAS QSVLHPLFAK GEEFAQTELK
LLAESARAKM TSQLTVELER LESLKAVNPN IRDEEITHLK DQMTELNGYL DDSLLQLDAV
RLVLVSHA
//
