ID F6CVB4_MARPP Unreviewed; 942 AA.
AC F6CVB4;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 27-MAR-2024, entry version 70.
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 OrderedLocusNames=Mar181_1177 {ECO:0000313|EMBL:AEF54224.1};
OS Marinomonas posidonica (strain CECT 7376 / NCIMB 14433 / IVIA-Po-181).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=491952 {ECO:0000313|EMBL:AEF54224.1, ECO:0000313|Proteomes:UP000009230};
RN [1] {ECO:0000313|EMBL:AEF54224.1, ECO:0000313|Proteomes:UP000009230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7376 / NCIMB 14433 / IVIA-Po-181
RC {ECO:0000313|Proteomes:UP000009230};
RX PubMed=23458837; DOI=10.4056/sigs.2976373;
RA Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA Detter J.C., Copeland A., Lu M., Bruce D., Detter C., Tapia R., Han S.,
RA Land M.L., Ivanova N., Mikhailova N., Johnston A.W., Sanchez-Amat A.;
RT "Complete genome sequence of Marinomonas posidonica type strain (IVIA-Po-
RT 181(T)).";
RL Stand. Genomic Sci. 7:31-43(2012).
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}.
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DR EMBL; CP002771; AEF54224.1; -; Genomic_DNA.
DR RefSeq; WP_013795700.1; NC_015559.1.
DR AlphaFoldDB; F6CVB4; -.
DR STRING; 491952.Mar181_1177; -.
DR KEGG; mpc:Mar181_1177; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR OrthoDB; 9814088at2; -.
DR Proteomes; UP000009230; 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; 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 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 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};
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 157..327
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 469..623
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT MOTIF 273..276
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01821"
FT BINDING 170..177
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01821"
SQ SEQUENCE 942 AA; 108638 MW; 286EF917ACB8650E CRC64;
MYQTGQRWSS RNEPDLGVGM IVDKQSKSFT LHFPDAETDR QYSHDQTSLV RRTLTIGDQL
HFQDDTFTVL EVEEIDNLIE YRISDQDDWL EESIIQFPRN DKNEIDSLLA LSPARRMWFD
LRRHTLEHQA ANAASPVRGL MGLKAELLPH QIYLAHDIAN RPKARALLCD EVGMGKTLEA
GLILHQRLLN GLCKRALILT PTNLQHQWLV EMLRRFHQPF SLINESVYED FMEGDDNPFE
QQPFVIAPID WASQHPKAAQ HMLDAEWDMV IVDEAHHLAW HPETPSIGYQ VVARLAASSE
SLLLLSATPE QTGEREHFSR LQLLDPDHYH NFERYQAQQQ EFKQAAELAE VILPFTQADH
GLEALNWSSE FASYLSEVKN KDWFIQLEKS QGEQQIEAAQ EAISWLIDRH GTGREMFRNT
RAAVGGFPDR YLHAYPLDNN ELFASATHHV RPEHDVAHGV WEKDPRWIWL KEFLECQADK
VLVICHTADM AQWLNDQLTF AGFQSADFHE QMPLIHRDRA AAYFADEDGA QILVCSEIGS
EGRNFQFSHH LVMYDLPEHP DLLEQRIGRL DRLGQLNDVQ IHVPYLKDSV QERLYNWYHR
ALNAFCRTTG SGDKVEDAFR ESLHAYLHGQ DDDLDLLKEA NVYHEALLKQ MEEGRNRLLE
MSSCRPDQAR QLIDQINHQA TKGLHHYIEQ VTHAFNIYTD CINDDPERAA WFLRPSSDMM
LEALPGIEEE GKMLMLDRRQ ASQREDVAFA TWEHPLITML MDEVQGFDSG KLTSAILPIA
ALPEGTVLVE SMFVIEATAH PRLKLAQSLP MTPMWQLSDS NGKFLHQQFT ADKWAEKLKG
VPNRVAEQWV AALRKNLIEV LQTHQLNAQD QARPIVHSAK AAYQHRCENE IDRLRELKAY
NSLIRDEDIA ALENNMQEGL VRIDEHQIRL DAIRIILTTK PE
//
