ID A0A0A3X6V8_9GAMM Unreviewed; 942 AA.
AC A0A0A3X6V8;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=GW12_03120 {ECO:0000313|EMBL:KGT48643.1};
OS Acinetobacter sp. HR7.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1509403 {ECO:0000313|EMBL:KGT48643.1, ECO:0000313|Proteomes:UP000032870};
RN [1] {ECO:0000313|EMBL:KGT48643.1, ECO:0000313|Proteomes:UP000032870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HR7 {ECO:0000313|EMBL:KGT48643.1,
RC ECO:0000313|Proteomes:UP000032870};
RA Ahn S., Kim B.-C.;
RT "Genome sequencing of Acinetobacter sp. strain HR7.";
RL Submitted (OCT-2014) 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:KGT48643.1}.
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DR EMBL; JPQO01000023; KGT48643.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A3X6V8; -.
DR STRING; 1509403.GW12_03120; -.
DR PATRIC; fig|1509403.3.peg.308; -.
DR eggNOG; COG0553; Bacteria.
DR Proteomes; UP000032870; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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 167..340
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 465..630
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 635..662
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 285..288
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 942 AA; 107440 MW; E5B49293B8AFDFAC CRC64;
MQQFAIGQRW LSDTETELGL GVLIDVDERS VSILFPKSDE TRVYARSNAP LSRIIFNAND
ELQDQEGNTW TVESVEDRNG VVRYHVVRTL EDGSEERKAL NETRVGATIQ LSKPLDRLLA
SQIDYKEWYD LRIEAMLMQA NMQNSPLRGL IGSRVGLIPH QLYIAHEVGQ RFAPRVLLAD
EVGLGKTIEA GLIIHQQLKT GRSERVLILV PDSLQYQWMI EMRRRFNLEF SLFDLTRTAS
IKEHDPDLNP FLTEQRIIAS IDLMIDHEDL REQALEAGFD LLVVDEAHHL MWSEEEGGND
RYDLVEEIAE KTPGVLLLTA TPEQLGVESH FARLRLLDPQ RFNSLDRFLD EEAQYQQTAK
IAEVLMSDMP LEEGHLTALK GLLGHEVEDT PEQRFRAIHE ILDRHGTGRI LFRNTREAIQ
GFPGRDCQPA PLPAPAGWSM DGKLREQMWP EESQLDGSWM ETDPRVPWLM EKLRTDLKHK
KVLLIARSGP VVEVLENALR LHAGIRTAMF HEGMSLLERD QAAAYFAEES YGAQILLCSE
IGSEGRNFQF ASDLILFDLP ANPDVLEQRI GRLDRIGQQN RIQIHVPYLV GTAQERMFRW
YNEALNIFSN ISPTAQTLQE NFIVELKDCL LADKGQQFED LLEEVTVQRQ ALEAELQEGR
DRLLEYNSCR PMVAQEIVNA LEDYDDNTTL PMFMKRFMAS TNIDFDEQSN GTVIIKPTDQ
MQVQGLTLDE EGMTATFYRD QAQIREDAQY LTLEHPFTES VMEMINTQGF GSTNVAVLKS
AALPQGSVLL EVWFKVDVVA PKALNLPASL PQQLIRVLLS EKGQDLSQKI APEILKPYLH
HLDGNSCRQV VKARREVIEA RYQQALELAR SALPQFKEQA KEAYGSKWQY EIDRLTYLKQ
FNPSIREDEI ARLQKLQKEG LSLLDGLAVT PEAIQVMVVV KP
//
