ID S7WU27_ACIJU Unreviewed; 942 AA.
AC S7WU27;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=L292_2285 {ECO:0000313|EMBL:EPR86676.1};
OS Acinetobacter junii CIP 107470 = MTCC 11364.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1217666 {ECO:0000313|EMBL:EPR86676.1, ECO:0000313|Proteomes:UP000018420};
RN [1] {ECO:0000313|EMBL:EPR86676.1, ECO:0000313|Proteomes:UP000018420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MTCC 11364 {ECO:0000313|EMBL:EPR86676.1,
RC ECO:0000313|Proteomes:UP000018420};
RA Khatri I., Singh N.K., Subramanian S., Mayilraj S.;
RT "Genome assembly of Acinetobacter junii MTCC 11364.";
RL Submitted (MAY-2013) 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:EPR86676.1}.
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DR EMBL; ASYZ01000041; EPR86676.1; -; Genomic_DNA.
DR AlphaFoldDB; S7WU27; -.
DR PATRIC; fig|1330047.3.peg.905; -.
DR eggNOG; COG0553; Bacteria.
DR Proteomes; UP000018420; 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; 107701 MW; A47A54C9E179671F CRC64;
MQQFAIGQRW LSDTETELGL GVLIDVDERS ISILFPKSDE TRVYARNNAP LSRIIFNVND
EVQDQEGSKW IVEAIEDRHG VLRYDVVRTL ENGEQERKSL NETRIGAQIQ LSKPLERLLA
SQIDYKEWYD LRIEAMLLQA QMHTSPLRGF LGARVGLIPH QLYIAHEVGK RFAPRVLLAD
EVGLGKTIEA GLIIHQQLKT GRSERILILV PDSLQYQWMI EMRRRFNLQF SLFDLTRTAS
IKEHDPDLNP FLTEQCIIAS VDLMVDHDDL REQAVEAGFD LLVVDEAHHL MWSEEDGGND
RYDLVEELAE QTAGVLLLTA TPEQLGVESH FARLRLLDPQ RFSSLDRFLD EEEQYQHTAK
IAEVLMSDEA LTEEHLVALD GLLGHRIDDQ PEQRMRAIHE LLDRHGTGRI LFRNTREAIQ
GFPGRDCQPA PLPAPEDWSF DGKMREQMWP EEGQLDGSWM ETDPRVPWLM EVLRKDLKHK
KVLLIARSGP VVEALENALR LHAGIRTAMF HEGMSLLERD QAAAYFAEDS YGAQILLCSE
IGSEGRNFQF ASDLILFDLP ANPDVLEQRI GRLDRIGQEN RIQIHVPYLV GTAQERMFRW
YNEALNIFSN ISPTAQTLQE NFIVELKDCL LADQGQTFED LLEEVNVQRQ ALEAELQAGR
DRLLEYNSCR PVVAQGIVQA LEDYDDNTTL PMFVKRFMSS TNIDFDEQSN GTVIIKPTDQ
MQVQGLTLDE EGMTATFYRD QAQIREDAQY LTLEHPFIES VMEMIRTQSF GSTNVALLKS
NALKQGSVLL EVWFKVDVVA PKALNLPSSL PKQLIRVLLS ENGQDLSAKI DPSILRPYLH
HLDGNSCRQV VKARRDVIET RYAQALDIAK TSLPELMQQA KEHYSSKWQY EIDRLTYLKQ
FNPSIRQDEI ERLQKFQKEG LGLLDGLSVT PEAIQVLVVV KP
//
