ID A0A095VTU3_9GAMM Unreviewed; 916 AA.
AC A0A095VTU3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=HRUBRA_00360 {ECO:0000313|EMBL:KGE04887.1};
OS Pseudohaliea rubra DSM 19751.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Pseudohaliea.
OX NCBI_TaxID=1265313 {ECO:0000313|EMBL:KGE04887.1, ECO:0000313|Proteomes:UP000029640};
RN [1] {ECO:0000313|EMBL:KGE04887.1, ECO:0000313|Proteomes:UP000029640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19751 {ECO:0000313|EMBL:KGE04887.1,
RC ECO:0000313|Proteomes:UP000029640};
RX PubMed=25414506;
RA Spring S., Fiebig A., Riedel T., Goker M., Klenk H.P.;
RT "Genome Sequence of Gammaproteobacterial Pseudohaliea rubra Type Strain DSM
RT 19751, Isolated from Coastal Seawater of the Mediterranean Sea.";
RL Genome Announc. 2:e01208-14(2014).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGE04887.1}.
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; AUVB01000013; KGE04887.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A095VTU3; -.
DR STRING; 1265313.HRUBRA_00360; -.
DR PATRIC; fig|1265313.6.peg.356; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR Proteomes; UP000029640; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000029640};
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 445..606
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 916 AA; 101809 MW; F38BD79E5A95E31A CRC64;
MVEFALGQRW VSHADAQLGL GIVVASEGPR VTLSFPAVGE ERTYAAGRAP LTRLRFKTGD
RLRTADGREL DVTAVTEREG LLFYRTADAA GEAHEVPEIE LDAFVQLTTP QQRLRNGHFD
RHEAFALRVA TCLQLDRLQR DPARGLLGPR TQLLPHQLYI AASVGRRHAP RVLLADEVGL
GKTIEAGMIL HQQLLTGRAS RVLVLVPEPL LHQWLVEMLR RFNLHFALFD AERLAAGDGE
NPFETEQLVL CAGDLLYEDP EAQADALAAP WDIVVVDEAH HLHWQPDAPG QDYRFVSALA
SASPGLLLLT ATPEQLGVES HFARLALIDP ARFHDLEVFR AEEAGYRQWS ELLEAIEAGR
RPASLPPGLD EGASDAVLIG RILDRHGTGR VLYRNTRASV GGFPARQLHA SALPAAGPAA
EPGALYPERH ARDDAWLAAE PRVAWLRDKL RALRPQKALV ICSTARCAEQ LEHYLHLRAG
IRCAAFHEGL SIIERDRAAA WFADAESGAQ ALVCSEIGSE GRNFQFAQHL VLFDLPRNPD
LLEQRIGRLD RIGQTGEVHI HVPYLAGTAQ ERLFRWLHEG LDIFRQNCPA GRPVFDAFRE
QLEATLEGTA DSDRLIAETR EATAAANRRL AEGRDRLLER NACRRPEAER IIEAIRDSER
SGELQAYFET LCDNLNVEHE YHSEGCLVLR PGEHMDTAHF PALPEDGRTV TFDRATALAR
EDMAFLSWEH PMVTEAMEAI LSTELGNAAL GTLKLRGVAT GTLLLECLYT VNASAPKSLQ
LQRFLSLSPQ RVLVDSRDRD LSQAVSHERL NQLVRRVDHA TAVGIIRQLQ GAVDERLAAA
AGLAEKHLTT LREDAARRAE NYLGEEITRL ESLQRVNPQV RDDEIEHLRW QREESLAAIA
RADLHLQAVR LVVVTA
//
