GenomeNet

Database: UniProt
Entry: A0KGL5
LinkDB: A0KGL5
Original site: A0KGL5 
ID   RAPA_AERHH              Reviewed;         955 AA.
AC   A0KGL5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, 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=AHA_0864;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS   13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC
RC   2358 / NCIMB 9240 / NCTC 8049;
RX   PubMed=16980456; DOI=10.1128/jb.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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}.
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; CP000462; ABK36250.1; -; Genomic_DNA.
DR   RefSeq; WP_011704808.1; NC_008570.1.
DR   RefSeq; YP_855406.1; NC_008570.1.
DR   AlphaFoldDB; A0KGL5; -.
DR   SMR; A0KGL5; -.
DR   STRING; 380703.AHA_0864; -.
DR   EnsemblBacteria; ABK36250; ABK36250; AHA_0864.
DR   KEGG; aha:AHA_0864; -.
DR   PATRIC; fig|380703.7.peg.868; -.
DR   eggNOG; COG0553; Bacteria.
DR   HOGENOM; CLU_011520_0_0_6; -.
DR   OrthoDB; 9814088at2; -.
DR   Proteomes; UP000000756; 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   CHAIN           1..955
FT                   /note="RNA polymerase-associated protein RapA"
FT                   /id="PRO_1000088348"
FT   DOMAIN          163..333
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   DOMAIN          478..642
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
FT   MOTIF           279..282
FT                   /note="DEAH box"
FT   BINDING         176..183
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01821"
SQ   SEQUENCE   955 AA;  107271 MW;  057A0606A509B8DB CRC64;
     MPFALGQRWI SDTETDLGLG TVVAVEGRMV TLLFPATGEN RMYAKEEAPV TRVSFNVGDQ
     IASHEDWTMT VEEVQEKDGL LIYVGVRTDN DEPVALKEVF LNNFIKFNKP QDRLFAGQID
     RMSRFTLRYE ALINQHQRRR NPTRGLAGGR VSLIPHQLYI AHEVGHRYAP RVLLADEVGL
     GKTIEAGMII HQQLLSGRAH RVLILLPETL QHQWLVEMLR RFNLHFSLFD EERCIEAFAD
     AENPFETEQL VICSLDFLRK KRRRFEQVLE AEWDLLVVDE AHHLEWSEEA PSRAYEMVEA
     LAEQVPGVLL LTATPDQLGH QSHFARLRLL DPERFYDYDA FLAEEQAYGQ VASAAQELLD
     GETLSDEAKR ILASQLEGLD LSDAAARQQA VAKLLDQHGT GRVLFRNSRA NIQGFPERHL
     NVYPMPLPEQ YKTAIKVMGM MGGNGGDLQT RALRYLYPEK IFQQFEGDNA TWTQFDPRVE
     WLLELLLSAR QQKVLVICSE AATAIALEEA LRTREGIRGA VFHEGMSILE RDKASAYFAQ
     QEGGAQVLLC SEIGSEGRNF QFASHLVLFD LPLNPDLLEQ RIGRLDRIGQ QNTVEIHVPY
     LEGTSQRALQ LWYHDGLDAF EQTCPTARPV FEAVRDELFE LLAANTGDQA PLDALLVKTR
     ELHEPLKARL EQGRDRLLEI HSSGGAAAQQ LVDKLAAEDD DTGMISFALK MFDEIGVNQD
     DRGENALVLT PGDHMLVSSF PGLPQDGMTI TFDRNTALSR DDMALLSWDH PMMRGGIDLI
     LGSEIGATSV ALLKNKALPI GSILLELIFV AESAAHPQLY RFMPPTPIRL LMDKNGQNLG
     EKVAFDAFNR QLTPVNRHLG SKLVTASQPV IHGLIGKGQA IAEELKGGIV DKARAQMAQT
     LQQDLDRLEA LKAVNPNVRD SELDYLRNLQ AELHHLIDQT QLKLDAIRFI VVTHN
//
DBGET integrated database retrieval system