ID RAPA_SALTY Reviewed; 968 AA.
AC Q8ZRV8;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 27-MAR-2024, entry version 122.
DE RecName: Full=RNA polymerase-associated protein RapA {ECO:0000255|HAMAP-Rule:MF_01821};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_01821};
DE AltName: Full=ATP-dependent helicase HepA {ECO:0000255|HAMAP-Rule:MF_01821};
GN Name=rapA {ECO:0000255|HAMAP-Rule:MF_01821}; Synonyms=hepA;
GN OrderedLocusNames=STM0096;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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:0000255|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:0000255|HAMAP-Rule:MF_01821}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. RapA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01821}.
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DR EMBL; AE006468; AAL19060.1; -; Genomic_DNA.
DR RefSeq; NP_459101.1; NC_003197.2.
DR RefSeq; WP_001116976.1; NC_003197.2.
DR AlphaFoldDB; Q8ZRV8; -.
DR SMR; Q8ZRV8; -.
DR STRING; 99287.STM0096; -.
DR PaxDb; 99287-STM0096; -.
DR GeneID; 1251614; -.
DR KEGG; stm:STM0096; -.
DR PATRIC; fig|99287.12.peg.100; -.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OMA; MSILERD; -.
DR PhylomeDB; Q8ZRV8; -.
DR BioCyc; SENT99287:STM0096-MONOMER; -.
DR Proteomes; UP000001014; 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; ATP-binding; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Reference proteome; Transcription;
KW Transcription regulation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..968
FT /note="RNA polymerase-associated protein RapA"
FT /id="PRO_0000207185"
FT DOMAIN 164..334
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT DOMAIN 490..685
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT MOTIF 280..283
FT /note="DEAH box"
FT BINDING 177..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
SQ SEQUENCE 968 AA; 109865 MW; D266E849A0977569 CRC64;
MPFTLGQRWI SDTESELGLG TVVAMDARTV TLLFPSTGEN RLYARSDSPV TRVMFNPGDT
ITSHEGWQLH IDEVKEENGL LVYVGTRLDT EETNVTLREV LLDSKLVFSK PQDRLFAGQI
DRMDRFALRY RARKFQSEQY RMPYSGLRGQ RTNLIPHQLN IAHDVGRRHA PRVLLADEVG
LGKTIEAGMI LHQQLLSGAA ERVLIIVPET LQHQWLVEML RRFNLRFALF DDERYTEAQH
DAYNPFETEQ LVICSLDFAR RNKQRLEHLC DAEWDLLVVD EAHHLVWSTD APSREYMAIE
QLAERVPGVL LLTATPEQLG MESHFARLRL LDPNRFHDFE QFVEEQKNYR PVADAVAMLL
AGNKLSNDEL NRLGDLIGEQ DIEPLLQAAN SDRDDAQAAR DELVSMLMDR HGTSRVLFRN
TRNGVKGFPK RELHTVKLPL PTQYQTAIKV SGIMGARKSP EDRARDMLYP EQIYQEFEGD
TGTWWNFDPR VEWLMGYLTS HRSQKVLVIC AKATTALQLE QVLREREGIR AAVFHEGMSI
IERDRAAAWF AEEDTGAQVL LCSEIGSEGR NFQFASNLVM FDLPFNPDLL EQRIGRLDRI
GQAHDIQIHV PYLEKTAQSV LVRWYHEGLD AFEHTCPTGR AIYDSAYASL INYLAAPEET
DGFDDLIKSC REQHEALKAQ LEQGRDRLLE IHSNGGEKAQ QLAQSIEEQD DDTNLIAFAM
NLFDIVGINQ DDRGDNLIVL TPSDHMLVPD FPGLPEDGCT ITFERDVALS REDAQFITWE
HPLIRNGLDL ILSGDTGSST ISLLKNKALP VGTLLVELVY VVEAQAPKQL QLNRFLPPTP
VRMLLDKNGN NLAAQVEFET FNRQLSAVNR HTGSKLVNAV QQDVHAILQL GETQIEKSAR
ALIDNARREA DEKLSGELSR LEALRAVNPN IRDDELAAID SNRQQVLESL NQAGWRLDAL
RLIVVTHQ
//
