ID Q604K8_METCA Unreviewed; 949 AA.
AC Q604K8;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 124.
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=hepA {ECO:0000313|EMBL:AAU91421.1};
GN Synonyms=rapA {ECO:0000256|HAMAP-Rule:MF_01821};
GN OrderedLocusNames=MCA2531 {ECO:0000313|EMBL:AAU91421.1};
OS Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylococcus.
OX NCBI_TaxID=243233 {ECO:0000313|EMBL:AAU91421.1, ECO:0000313|Proteomes:UP000006821};
RN [1] {ECO:0000313|EMBL:AAU91421.1, ECO:0000313|Proteomes:UP000006821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33009 / NCIMB 11132 / Bath
RC {ECO:0000313|Proteomes:UP000006821};
RX PubMed=15383840; DOI=10.1371/journal.pbio.0020303;
RA Ward N.L., Larsen O., Sakwa J., Bruseth L., Khouri H.M., Durkin A.S.,
RA Dimitrov G., Jiang L., Scanlan D., Kang K.H., Lewis M.R., Nelson K.E.,
RA Methe B.A., Wu M., Heidelberg J.F., Paulsen I.T., Fouts D.E., Ravel J.,
RA Tettelin H., Ren Q., Read T.D., DeBoy R.T., Seshadri R., Salzberg S.L.,
RA Jensen H.B., Birkeland N.K., Nelson W.C., Dodson R.J., Grindhaug S.H.,
RA Holt I.E., Eidhammer I., Jonasen I., Vanaken S., Utterback T.R.,
RA Feldblyum T.V., Fraser C.M., Lillehaug J.R., Eisen J.A.;
RT "Genomic insights into methanotrophy: the complete genome sequence of
RT Methylococcus capsulatus (Bath).";
RL PLoS Biol. 2:1616-1628(2004).
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; AE017282; AAU91421.1; -; Genomic_DNA.
DR RefSeq; WP_010961752.1; NC_002977.6.
DR AlphaFoldDB; Q604K8; -.
DR STRING; 243233.MCA2531; -.
DR KEGG; mca:MCA2531; -.
DR eggNOG; COG0553; Bacteria.
DR HOGENOM; CLU_011520_0_0_6; -.
DR Proteomes; UP000006821; 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; 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:UP000006821};
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 167..336
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 479..635
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT MOTIF 282..285
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01821"
FT BINDING 180..187
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01821"
SQ SEQUENCE 949 AA; 107399 MW; 7699E3C26ED64804 CRC64;
MAGPLHTLRS GQRWISDTEP ELGLGTVVGV EHDRVTVSFI ASGERRIYAV GNAPLSRVRF
AAGDRVESVD GWSMQVEEVE EQDGLLVYLG KDADGKPRTL EEIELNPFLQ FNRPQDRLLS
GQIDPGDVFR LRIETGEKLA RLEQSPVLGL VGPRTALIPH QLYIAHEVAS RHAPRVLLAD
EVGLGKTIEA GLIIHHRVLT GRTEKVLILV PNMLLHQWLV EMLRRFNLRF SLIGEDAYED
AAEEGSPFKD VNLALSSLDF ILKDPERRRY VLDVAWDMVV IDEAHHLEWT PEKPSPAYAF
VEMLARRTPG LLLLTATPEQ LGKLGHFARL RLLDPDRFFD FEQFRQEEQE YTALAGVIDK
LLDSPRLDAD TLGQLQHFLR HDRADALVGD LNDPEHAAAA RNALIQLLLD RHGTGRVLFR
NTRNTVHGFP SRLLHGRPLP LPEHYRTQKA SLEARLWPES ARPDPDWWRH DPRVHWLLDI
AQRLKPSRSK LLVICHRQQT AVDLENALRT LGGVRAAVFH EGMSIIARDR AAAWFAEEEE
GAQVLVCSEI GSEGRNFQFA HHLVLFDLPL DPNLLEQRIG RLDRIGQHHS IDIHVPYFED
SAQEILFRWY HEGLDAFHRP AAAGAAVFAR LGDELRRVLL APDTHAGITL IQDTRTLAET
IEAKLHAGRD RLLELNSCRP EPANRLVEAV AAWDRDTALW PWLEAVCDAY GVVVEEHSTD
CYILRPGEHL RVPKFPELPE DGVTVTLSRD VALAREDMVF LSWEHPLVRG AIDLVLNGEH
GNASLGFVSH PALASGQMLL ETFHRIECPA PRRLQLFRFL PTTQLRTLLD HRGQDLGRIA
MAEFDERPQT FEPANVRAFV RSQKPNLEKL LALAETRAGT RLTEIVADSS RRMLDEMTNE
LKRLAALRSV NPSVRQEELD RLKDDAVEMH GYLQAARLRL DAVRLLITV
//
