ID A8T954_9VIBR Unreviewed; 969 AA.
AC A8T954;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 27-MAR-2024, entry version 80.
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=AND4_13345 {ECO:0000313|EMBL:EDP58148.1};
OS Vibrio sp. AND4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=314289 {ECO:0000313|EMBL:EDP58148.1, ECO:0000313|Proteomes:UP000005159};
RN [1] {ECO:0000313|EMBL:EDP58148.1, ECO:0000313|Proteomes:UP000005159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AND4 {ECO:0000313|EMBL:EDP58148.1,
RC ECO:0000313|Proteomes:UP000005159};
RX PubMed=20436956; DOI=10.1371/journal.pbio.1000358;
RA Gomez-Consarnau L., Akram N., Lindell K., Pedersen A., Neutze R.,
RA Milton D.L., Gonzalez J.M., Pinhassi J.;
RT "Proteorhodopsin phototrophy promotes survival of marine bacteria during
RT starvation.";
RL PLoS Biol. 8:E1000358-E1000358(2010).
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:EDP58148.1}.
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DR EMBL; ABGR01000014; EDP58148.1; -; Genomic_DNA.
DR RefSeq; WP_009843564.1; NZ_ABGR01000014.1.
DR AlphaFoldDB; A8T954; -.
DR OrthoDB; 9814088at2; -.
DR Proteomes; UP000005159; 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}; 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 164..334
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 492..646
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT COILED 905..957
FT /evidence="ECO:0000256|SAM:Coils"
FT MOTIF 280..283
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01821"
FT BINDING 177..184
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01821"
SQ SEQUENCE 969 AA; 109902 MW; 9EED61B648753C89 CRC64;
MTFALGQRWI SDTESDLGLG TVVAVDTRTV TLMFAASEEN RVYARSDAPV TRVTFNVGDV
IDCQEGWSLK VEEVLEDEGL YTYFGTREDT QETAIVLREI FLSNHIRFNK PQDKLYAGQI
DRMDNFVLRY RALQNQFEQH KSPMRGLCGI RAGLIPHQLY IAHEVGRRYA PRVLLADEVG
LGKTIEAGMI IHQQVLSGRA ERILIVVPET LQHQWLVEMM RRFNLHFSIF DEERCIEAFS
EAENPFDTQQ YVLCSLDFLR KSRKRFEQAL EGEWDLLVVD EAHHLEWSQD KPSREYQVVE
GLAERTAGVL LLTATPEQLG RESHFARLRL LDPDRFYDYD AFVEEEEQYA PVADAITSLF
SGEKLPNDAK NQITELLCEQ DVEPLFRIIE SDSDEEAKAL ARQELIDNLM DRHGTGRVLF
RNTRAAIKGF PKRNVHLMPM DIPQQYTTSM RVSGMIGGKM TQEARAVKNL YPEEIFQEFE
GEDSSWWQFD SRVNWLLEKV KEKRSDKVLV IASRASTALQ LEQALREREG IRATVFHEGM
TILERDKAAA YFAQEEGGAQ VLICSEIGSE GRNFQFANQL VMFDLPFNPD LLEQRIGRLD
RIGQQRDIDI HVPYLKDTSQ AILARWFDEG LNAFAETCPT GRAVYDKYAD ALIEMLASGD
VSNLDQVIEE SAKMNQALRS QLEQGRDRLL EMHSNGGEKA QQIVEKISSK DGDTNLVAFA
LSLFDTIGLN QDDKGENALV VTPSEHMMVP SYPGLPYEGA TITFDRDTAL SREDMHFISW
EHPMIQGGID LLMSEGVGAS AVSLLKNKAL PVGTILLELV YAVDAQAPKR SGIARFLPKT
PIRMMMDARG NDLSSQVDFE GFNRQLSPVN RHLGSKLVTS VQKDIHGLIE AGDALVEQKV
EEVRQQAHQD MQQSLNAELE RLQALKAVNP NIRDEEIDVI EEQIKELTGY INQAQVQLDS
LRLIVVSHN
//
