ID A0A1Z4BYM5_9GAMM Unreviewed; 941 AA.
AC A0A1Z4BYM5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=AADEFJLK_00842 {ECO:0000313|EMBL:POZ53801.1}, CEK71_10150
GN {ECO:0000313|EMBL:ASF46407.1};
OS Methylovulum psychrotolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylovulum.
OX NCBI_TaxID=1704499 {ECO:0000313|EMBL:ASF46407.1, ECO:0000313|Proteomes:UP000197019};
RN [1] {ECO:0000313|EMBL:ASF46407.1, ECO:0000313|Proteomes:UP000197019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HV10_M2 {ECO:0000313|EMBL:ASF46407.1,
RC ECO:0000313|Proteomes:UP000197019};
RA Mateos-Rivera A.;
RT "Genome Sequencing of the methanotroph Methylovulum psychrotolerants str.
RT HV10-M2 isolated from a high-altitude environment.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:POZ53801.1, ECO:0000313|Proteomes:UP000237423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sph1 {ECO:0000313|EMBL:POZ53801.1,
RC ECO:0000313|Proteomes:UP000237423};
RA Oshkin I.Y., Miroshnikov K., Belova S.E., Korzhenkov A., Toshchakov S.V.,
RA Dedysh S.N.;
RT "Draft Genome Sequence of Methylobacter psychrotolerans Sph1T, an Obligate
RT Methanotroph from Low-Temperature Environments.";
RL Submitted (NOV-2017) 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}.
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DR EMBL; CP022129; ASF46407.1; -; Genomic_DNA.
DR EMBL; PGFZ01000001; POZ53801.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4BYM5; -.
DR KEGG; mpsy:CEK71_10150; -.
DR OrthoDB; 9814088at2; -.
DR Proteomes; UP000197019; Chromosome.
DR Proteomes; UP000237423; 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; 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:UP000197019};
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..346
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 470..623
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT MOTIF 292..295
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 941 AA; 106402 MW; 0C1167B40DA5EBFD CRC64;
MESFIPGQRW ISNTESELGL GLILDVSFNR VTVLYLASDE RRIYARDNAP LTRVVFSVGD
TIESVDEDKL TVTEVIENNG LMTYIGKTAD GEAMQFEEVE LNHRIQFNKP QDRLFIGQID
PNDWFSLRYE TWQRLRQHQQ SPVKGLLGSR ASLIPHQVFI AHESANRIAP RIMLADEVGL
GKTIEAGLIL HHRLINGLSQ RVLIIVPESL LHQWLVEMLR RFNLRFSLFD EARCLGELGD
DGMDEDDADK AVLSGNPFVN EQLVLCSQQF FAQHPLRQQQ ALQAGWDMVI VDEAHHLAWS
EQAASSEYLF VEQLALATPS LILLTATPEQ LGKESHFARL RLLDPDRFYS FAAFLAEEKQ
FEPVADAAKI LLADKPLAEA DSALLAGLLK DDNVGTLLKN LADSEKSAAA RAALIKILLD
HHGTGRILFR NSRQTVQGFP ERERHGYPLE GDENTADLQK DPRYLWLVNT LISATSALRD
QKALLICKHA QTAVDLELTL RVRGGIASAV FHEGMSIIER DRAAAYFADQ DSAARLLICS
EIGSEGRNFQ FVHHLILWDL PTNPDLLQQR IGRLDRIGQQ HVIQIHIPYL EHSRQALLYR
WYDEGMNAFR ANCSAARPVA DVLADELEAM LFQDEAQIEA FIAKTQALGR EIAEQLHNGR
DQLLELNSFR KDEAELWVEQ LKRYEKEALL WPYMEAVFEC YGVDTEFHSP DCFIVRPSDH
LRIAHFPGLD EDGVTVTVKR ACALAREDMQ FLTWEHPMVT AAMDLVLSSE TGNAVVSVVK
HRDLRPGQFL LECLFIVECS APAQLQIGRF LPPTPIRILI DQHQQDLTEV FSHQQLPETG
KAFDKQQIAA FLNSQRKPLS KLLYNAEELA RVRMQALTAE ANTTMLESLS AEVKRMARLK
KVNPSIKAEE IEQLKDLTML AHESIQAAQL RLDAVRFVIA S
//
