ID A0A0W1AHB6_9GAMM Unreviewed; 950 AA.
AC A0A0W1AHB6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 37.
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:KTD80716.1};
GN Synonyms=rapA {ECO:0000256|HAMAP-Rule:MF_01821};
GN ORFNames=Lwor_0959 {ECO:0000313|EMBL:KTD80716.1};
OS Legionella worsleiensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45076 {ECO:0000313|EMBL:KTD80716.1, ECO:0000313|Proteomes:UP000054662};
RN [1] {ECO:0000313|EMBL:KTD80716.1, ECO:0000313|Proteomes:UP000054662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49508 {ECO:0000313|EMBL:KTD80716.1,
RC ECO:0000313|Proteomes:UP000054662};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) 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 -!- 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:KTD80716.1}.
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DR EMBL; LNZC01000009; KTD80716.1; -; Genomic_DNA.
DR RefSeq; WP_058492781.1; NZ_UGPA01000001.1.
DR AlphaFoldDB; A0A0W1AHB6; -.
DR STRING; 45076.Lwor_0959; -.
DR PATRIC; fig|45076.6.peg.1045; -.
DR OrthoDB; 9814088at2; -.
DR Proteomes; UP000054662; 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:UP000054662};
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 162..341
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 471..618
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT MOTIF 287..290
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01821"
FT BINDING 175..182
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01821"
SQ SEQUENCE 950 AA; 108079 MW; 3F9C3EF7E3538237 CRC64;
MTFTIGQRWI SNTESQLGLG IITEVGGRHV NINFPAAEED RIYAIDNAPL SRIIFKIGEE
ITTNEDKTLH VTEVHDFKGL IIYTALDAKG QEQAINEMAL NCFISLSTPQ QRLFSGLLDK
LNSFKLRIDT LNHISRLQQS KVRGLLGSRT NHLLHQVYIA SEVAQRHAPR VLLADEVGLG
KTIEAGMILH YQLHTGRASR VLIIVPDSLI HQWLVEMIRK FNLYFSIFDK NRFQSTLDAE
NEAHNPGGES NIFETEQLVL CSLDFLMSNE EARQHALAAQ WDLLIVDEAH HLHWSEELAG
PEYEFIEQLS AQSKGLLLLT ATPEQVGIQS HFARLRLLDP SRFYDFKLFK KEEESYQKVN
RLVQRLIDYK ETQQTDTLDA SSRSSLAEYL GQDISDSIST NIKNLLDRHG TGRVLFRNTR
AAIKGFPKRN VTAYPLSNSP LYTAINAIEN TLNLYPETPL DNDVWLLNDP RVQWLASKIN
ELYPEKVLII CAKAKTALAL EQFLKLKAGI RSTAFHEGLT IIERDKAAAY FADQEQGAQA
LICSEIGSEG RNFQFAHHLV LFDLPLNPDL LEQRIGRLDR IGQKNTIEIH VPYLTDTAQE
ILFRWYHEGI NLFQQSCSVG YSVYEQFAER LLPILKANNL GTNPEPLNTL IEDTKRFTLQ
INQALQEGRD QLLELNSCNP VIAEQIIAEI EAEESSIELE NYMAKVFHEF GIDHEYHSEL
AEILRPTEHM KTSHFPGLQE DGVTVTYSRS KALVREDMEF LSWEHPMVSE SMEMILNSEV
GNATLTTISV KSIAPGTLFL ETFYTINGAA PKYLQLDRFL PFTPLRILMD VSGKNLSKVL
DYNQLNAMCE PVKRHLGYPI VKQISSDIES ILKNCNQIAE KQMNEVIEHA KMNMVQSLSA
EISRLESLQQ VNPAIRAEEI EFFKEQMSEC ERYMNSAALK LQAIRVVINK
//
