ID A0A1M5DFI0_9GAMM Unreviewed; 978 AA.
AC A0A1M5DFI0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=SAMN02745148_03219 {ECO:0000313|EMBL:SHF65729.1};
OS Halomonas ilicicola DSM 19980.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1121942 {ECO:0000313|EMBL:SHF65729.1, ECO:0000313|Proteomes:UP000184346};
RN [1] {ECO:0000313|EMBL:SHF65729.1, ECO:0000313|Proteomes:UP000184346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19980 {ECO:0000313|EMBL:SHF65729.1,
RC ECO:0000313|Proteomes:UP000184346};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQUJ01000017; SHF65729.1; -; Genomic_DNA.
DR RefSeq; WP_072824712.1; NZ_FQUJ01000017.1.
DR AlphaFoldDB; A0A1M5DFI0; -.
DR STRING; 1121942.SAMN02745148_03219; -.
DR OrthoDB; 9814088at2; -.
DR Proteomes; UP000184346; 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}; Reference proteome {ECO:0000313|Proteomes:UP000184346};
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..658
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 978 AA; 109521 MW; BC83F59E7AD34E31 CRC64;
MSVFTPGQRW ISDGEAELGL GTILNCDQRS VTVLFAASQE TRTYSVRQAP LTRVAFGSGD
RIAAAEGWHL IVDDIEEVDG LLVYRGETDT GEPAELPEAR IADGMQFNQA RDRLLTGQID
RNDWFDLRFR TLHHHHRTEQ NPALGLAGPK IDLIPHQLYI ADEVSRRHAP RVLLADEVGL
GKTIEAGLVL HRLLLSGRAE RALILVPDNL THQWLVELLR RFALEVTLLD EQQSQAHGEA
NPFESGQLIL ASQQWLFANP HRQAQATACD WDLLIVDEAH HLDWTPSASG PGYACVERLA
GRIPGLLLVT ATPEQMGLES HFARLRLLDP DRYHDLSRFR LEEAGYVQVA AAIDALDRLP
DDNEATDIVA AEIDDADSQA LLATLSDPES ADTQRDKARR QLREHLLDRH GTGRVMFRNS
RRHVGGFPER HLHATRLELP SAYRRLLHTF LHGDDALDEL LVDTGLDYPD VLLYLEATYR
ALGDDPRHAE PWWQIDPRVT WLLELLTGAG RDKLLVITHD RDTAVDLAEA LRVLGGVFAP
VFHEGMSLVE RDRAAAAFAD EEYGSQLMVC SEIGSEGRNF QFCRHLVMFD LPQHPDQLEQ
RIGRLDRIGQ HHAIEIHVPV FAASPMEQLL RWYRQGMDAF SAPHGVGSSL YDAFGDALAD
AFLDAESLDE IIVETRALFE TRLAERDAGR NRLLELNACR PDRAEAVIAA IRELDDDPAL
KRYLDQALDI FGVDSQDLDE GLMHLRAGPH MLDGLPGLAK GEEGFTATSS RQRALVRDDV
QHLSWEHPLV REMMGRILDG AMGNTALALL NHPSIPAGRL MVELVFRTYC PAPRRLHVNR
FLPPTAIRVL LDESGANLSS RVSFTGLAKN LRKVKKAVAR DLIKSRHDQL RELLTQGEGE
AERELPTIIE VAQQRMRAEL DDELTRLKAL ARHNPAVRDD EVQALQDERA ALDAAIDGTR
LRLDAVRVIV TVDDSTKR
//
