RAPA_SHIDS
ID RAPA_SHIDS Reviewed; 968 AA.
AC Q32K36;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
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}; OrderedLocusNames=SDY_0083;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000034; ABB60321.1; -; Genomic_DNA.
DR RefSeq; WP_001117038.1; NC_007606.1.
DR RefSeq; YP_401810.1; NC_007606.1.
DR AlphaFoldDB; Q32K36; -.
DR SMR; Q32K36; -.
DR STRING; 300267.SDY_0083; -.
DR EnsemblBacteria; ABB60321; ABB60321; SDY_0083.
DR KEGG; sdy:SDY_0083; -.
DR PATRIC; fig|300267.13.peg.93; -.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OMA; MSILERD; -.
DR Proteomes; UP000002716; 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 transcription, DNA-templated; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR000330; SNF2_N.
DR InterPro; IPR040765; Tudor_1_RapA.
DR InterPro; IPR040766; Tudor_2_RapA.
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; SSF52540; 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 CHAIN 1..968
FT /note="RNA polymerase-associated protein RapA"
FT /id="PRO_1000088393"
FT DOMAIN 164..334
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT DOMAIN 490..662
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; 109809 MW; 593C7AE3D8D63108 CRC64;
MPFTLGQRWI SDTESELGLG TVVAVDARTV TLLFPSTGEN RLYARSDSPV TRVMFNPGDT
ITSHDGWQMQ VEEVKEENGL LTYIGTRRDT EESGVALREV FLDSKLVFSK PQDRLFAGQI
DRMDRFALRY RARKYSSEQF RMPYSGLRGQ RTSLIPHQLN IAHDVGRRHA PRVLLADEVG
LGKTIEAGMI LHQQLLSGAA ERVLIIVPET LQHQWLVEML RRFNLRFALF DDERYAEAQH
DAYNPFDTEQ LVICSPDFVR RSKQRLEHLC EAEWDLLVVD EAHHLVWSED APSREYQAIE
QLAEHVPGVL LLTATPEQLG MESHFARLRL LDPNRFHDFA QFVEEQKNYR PVADAVAMLL
AGNKLSNDEL NMLGEMIGEQ DIEPLLQAAN SDSEDAQSAR QELVSMLMDR HGTSRVLFRN
TRNGVKGFPK RELHTIKLPL PTQYQTAIKV SGIMGARKSA EDRARDMLYP ERIYQEFEGD
NATWWNFDPR VEWLMGYLTS HRSQKVLVIC AKAATALQLE QVLREREGIR AAVFHEGMSI
IERDRAAAWF AEEDTGAQVL LCSEIGSEGR NFQFASHMVM FDLPFNPDLL EQRIGRLDRI
GQAHDIQIHV PYLEKTAQSV LVRWYHEGLD AFEHTCPTGR TIYDSVYNDL INYLASPDQT
EGFDDLIKNC REQHEALKAQ LEQGRDRLLE IHSNGGEKAQ ALAESIEEQD DDTNLIAFAM
NLFDIIGINQ DDRGDNMIVL TPSDHMLVPD FPGLSEDGIT ITFDREVALA REDAQFITWE
HPLIRNGLDL ILSGDTGSST ISLLKNKALP VGTLLVELIY VVEAQAPKQL QLNRFLPPTP
VRMLLDKNGN NLAALVEFET FNRQLNAVNR HTGSKLVNAV QQDVHAILQL GEAQIEKSAR
ALIDAARNEA DEKLSAELSR LEALRAVNPN IRDDELTAIE SNRQQVMESL DQAGWRLDAL
RLIVVTHQ
