ID I1DXV6_9GAMM Unreviewed; 967 AA.
AC I1DXV6;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
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 ECO:0000313|EMBL:GAB58884.1};
GN ORFNames=RNAN_1872 {ECO:0000313|EMBL:GAB58884.1};
OS Rheinheimera nanhaiensis E407-8.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=562729 {ECO:0000313|EMBL:GAB58884.1, ECO:0000313|Proteomes:UP000004374};
RN [1] {ECO:0000313|EMBL:GAB58884.1, ECO:0000313|Proteomes:UP000004374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E407-8 {ECO:0000313|EMBL:GAB58884.1,
RC ECO:0000313|Proteomes:UP000004374};
RX PubMed=23209246; DOI=10.1128/JB.01922-12;
RA Zhang X.-Y., Zhang Y.-J., Qin Q.-L., Xie B.-B., Chen X.-L., Zhou B.-C.,
RA Zhang Y.-Z.;
RT "Genome Sequence of the Protease-Producing Bacterium Rheinheimera
RT nanhaiensis E407-8T, Isolated from Deep-Sea Sediment of the South China
RT Sea.";
RL J. Bacteriol. 194:7001-7002(2012).
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:GAB58884.1}.
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DR EMBL; BAFK01000009; GAB58884.1; -; Genomic_DNA.
DR RefSeq; WP_008220993.1; NZ_BAFK01000009.1.
DR AlphaFoldDB; I1DXV6; -.
DR STRING; 562729.RNAN_1872; -.
DR OrthoDB; 9814088at2; -.
DR Proteomes; UP000004374; 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:UP000004374};
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 163..333
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 489..639
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT MOTIF 279..282
FT /note="DEAH box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01821"
FT BINDING 176..183
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01821"
SQ SEQUENCE 967 AA; 108521 MW; 1491EDE8AA9B36A0 CRC64;
MSFALGQRWI SDTESDLGLG TVVAIEGRHL TLLFPASGET RLYAQADAPL TRVKFNVGDE
IASADGFKLL VAAIKQQHDN LVYCGKRLDD DSYVELRETF LDHFISFNQP QDRLFAGQID
RFDWFTLRYQ AWQQLHQQQQ NPLQGLTGAR VSLIAHQLHI ANEVAKRHAP RVLLADEVGL
GKTIEAGLII HQQLISGLAS RVLIVVPEAL QHQWLVEMLR RFNLRFSVFD QERCEQSALD
VANPFDTEQL VLCSLSFLQN QPRWHQLACD SQWDLLVVDE AHHLQWSEHA PSEAYQRIDA
LAQQTAGLIL LTATPDQLGH ESHFARLKLL DPARFHSYDA FLQEEQQYQQ VAAVATPLLA
QSPLTPAEQT ALQQMLTETD ISAELSLLQQ GDAQQQQQAR QKLLAQLLDR HGTGRILFRN
SRASIKGFPK RSAHLYPLAL PEQYQTALKV HFSLNPDLSE AERVQANLFP EQVLQQLDDS
SCWWQFDPRV ETLISLLKQH KQEKFLLICA HARTAIALEE AVRQREGIRA AVFHEGMSIV
ERDKAAAYFA QEEYSAQLLL CSEIGSEGRN FQFAHHLVLF DLPLNPDLLE QRIGRLDRIG
QRADIQLHLP HFANQAQQLL LDWYQQGLDA FAHTCQTGRS VFEQVCDRLI PLLAQPVADQ
PAMATLIRDS QQLNQQLKTR LEQGRDKLLE IHSAGGEQAK QLAQAIAAQD NDTALPLLMF
KAWDLLGINQ DDRSDTSIIL TPSEQMQGSY PWLGDEGVTV TFDRATALAE EDIQLLSWDH
PMVRGTLDIL TTEPHGSSSV ALLANKALPV GSYLLELNFI IEASAPPALQ LPRYLPATPL
RLLLDKNANN LSAKVSFEQL NKQLKPVGRQ TGSKLAGALQ QLVHPLLAKA TEIATTQMAN
VISSAQQSVS QTLGAQQQRL TALRQLNPSV RQDEIDALAK QQQQLTDYIS KARLKLDAIR
LIVVSHD
//
