ID A0A5Q0BFI5_9GAMM Unreviewed; 949 AA.
AC A0A5Q0BFI5;
DT 22-APR-2020, integrated into UniProtKB/TrEMBL.
DT 22-APR-2020, sequence version 1.
DT 18-JUN-2025, entry version 25.
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 ECO:0000313|EMBL:QFY41892.1};
GN ORFNames=F6R98_03965 {ECO:0000313|EMBL:QFY41892.1};
OS Candidatus Methylospira mobilis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Methylococcales; Methylococcaceae; Candidatus Methylospira.
OX NCBI_TaxID=1808979 {ECO:0000313|EMBL:QFY41892.1, ECO:0000313|Proteomes:UP000325755};
RN [1] {ECO:0000313|EMBL:QFY41892.1, ECO:0000313|Proteomes:UP000325755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shm1 {ECO:0000313|EMBL:QFY41892.1,
RC ECO:0000313|Proteomes:UP000325755};
RA Oshkin I.Y., Dedysh S.N., Miroshnikov K., Danilova O.V., Hakobyan A.,
RA Liesack W.;
RT "Ecophysiology of the spiral-shaped methanotroph Methylospira mobilis as
RT revealed by the complete genome sequence.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
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; CP044205; QFY41892.1; -; Genomic_DNA.
DR RefSeq; WP_153247876.1; NZ_CP044205.1.
DR AlphaFoldDB; A0A5Q0BFI5; -.
DR FunCoup; A0A5Q0BFI5; 131.
DR KEGG; mmob:F6R98_03965; -.
DR InParanoid; A0A5Q0BFI5; -.
DR OrthoDB; 9814088at2; -.
DR Proteomes; UP000325755; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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-like.
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 NCBIfam; NF003426; PRK04914.1; 1.
DR PANTHER; PTHR45766; DNA ANNEALING HELICASE AND ENDONUCLEASE ZRANB3 FAMILY MEMBER; 1.
DR PANTHER; PTHR45766:SF6; 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:UP000325755};
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 477..630
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 949 AA; 107711 MW; 9F82CBA637232C25 CRC64;
MPTFIPGQRW ISETEPELGL GMVLEATRAR VTVLFIASNE RRTYAADNAP LNRVRFVVGD
TIESADGWQI CVSRIQEQAG LITYIGADLK NKPRELEETE LSHNIQFNRP QDRLFSGQID
TSEQFKLRCR TRDALIALEQ SPIRGLAGAR AGLIPHQLYI AHEVAGRHAP RVLLADEVGL
GKTIEACLIA HHQILSGRAE RVLILVPEPL LHQWLVELRR RFNLNFSLYD EERYWQTPEG
NPFLSEQWIL TSLTLFSAEP ERKAMLLGAG WDLCIVDEAH HLDWSPETPG EDYLLVEQLA
RKTPGLLLLT ATPEQFGKEN HFARMKLLDP DRFSSYEAFI AEEANYIPLA RLIERLTATT
APDEKTREQL RGTLCHDRAE QLIAGLDDPE TNEQSRDELV RLLLDRHGTG RILFRNTRAT
VKGFPARQPK PYPLTLPDAY KTDTDTTLAA LLHPETSYRT LQDSDTPWWK VDPRVNWLCK
LLSELRPAKI LVICATQATA MELDAAINRL TTVGSTIFHE GMSIMERDRA AAWFADEEDG
AQVLVCSEIG SEGRNFQFAH HLVLFDLPLN PELLEQRIGR LDRIGQTSAI QLHIPYLRQS
AQETLFRWYH EGLDAFTHHG QASMEVYDRL SAELHQTLLA PVRQEKLEAL LARTRKLRDE
VLTRLHDGRD RLLEFNSCRS HAAETLADAI RAQDEDNNLW PWLESVFEVY GVNVEEHSEH
CHILLPGDHM PISRFPELPE EGVTATRNRE TALAREDMIF LTWEHPMVRG AIDLILGSEQ
GNAAFALVQH EDLEPGQLLL DAVYLLECAA PKRLQAYRHM PQTLVRVLVD SEAGVINDLP
PEDLIEIPRR PDREALGQMF QAQRKAIETM IRLSEKTAKN AMPSMVAIAL KTMLDEATAE
LQRLAALKKV NPSVRQDELD KLKADTLETH GHIQATRLRL DALRILLAV
//
