ID A0A126T118_9GAMM Unreviewed; 920 AA.
AC A0A126T118;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-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=rapA {ECO:0000256|HAMAP-Rule:MF_01821};
GN ORFNames=JT25_004635 {ECO:0000313|EMBL:AMK75778.1};
OS Methylomonas denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=1538553 {ECO:0000313|EMBL:AMK75778.1, ECO:0000313|Proteomes:UP000030512};
RN [1] {ECO:0000313|EMBL:AMK75778.1, ECO:0000313|Proteomes:UP000030512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJG1 {ECO:0000313|EMBL:AMK75778.1,
RC ECO:0000313|Proteomes:UP000030512};
RX PubMed=25580993; DOI=10.1111/1462-2920.12772;
RA Kits K.D., Klotz M.G., Stein L.Y.;
RT "Methane oxidation coupled to nitrate reduction under hypoxia by the
RT Gammaproteobacterium Methylomonas denitrificans, sp. nov. type strain
RT FJG1.";
RL Environ. Microbiol. 17:3219-3232(2015).
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}.
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DR EMBL; CP014476; AMK75778.1; -; Genomic_DNA.
DR RefSeq; WP_036273634.1; NZ_CP014476.1.
DR AlphaFoldDB; A0A126T118; -.
DR STRING; 1538553.JT25_004635; -.
DR KEGG; mdn:JT25_004635; -.
DR OrthoDB; 9814088at2; -.
DR Proteomes; UP000030512; Chromosome.
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};
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:UP000030512};
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..331
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 445..602
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT MOTIF 277..280
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 920 AA; 104349 MW; 85130859BBA17CE0 CRC64;
MNEFIPGQRW ISNTESELGL GMVMDAEFNR VTVLFLATGD RRVYARDNAP LTRVQFNEGD
VIESADYAKI SVQQVQQHNG LLTYIGIDED GQLQQIDEME LNHHIQFNKP QDRLFTGQFD
PTAWFLLRHE TWRRQQQHQQ AATKGLQGAR ASLIPHQLYI AHQAASRALP RIMLADEVGL
GKTIEAGLII QHRLINGLSK RVLILVPESL LHQWLVEMLR RFNLRFSIFD ESRCFASPDE
NPFLSEQLVL CSQRFFADSA HRQQQALDAG WDLVVVDEAH HLEWSEDAPS ADYLFVEQLA
LASPGLILLT ATPEQLGKES HFARLRLLDP DRFYRFEQFL REESQFEPVA RLANLLISGE
VLDAEQQGQL KNLLKQDNVD KLLQQVNDTQ ANAREELIKL LLDHHGTGRI LFRNSRQTVQ
GFPDRQRHAY PLQGDDTADL ANSPYLYWLV GQLKALGDEK ALLICKRAET AIQLEQLLRQ
HVGHTAAVFH EGMSIVESDR AAAFFADEES RAQVLICSEI GSEGRNFQFV RHLFLFDLPE
NPDLLQQRIG RLDRIGQKHV IQIHIPYLVD SAQHVLFRWY DEGLEAFRHN CSGAAQVLKL
LGDARDSALL SRDAAAVEAL IATTKTLSSQ VEDELHKGRD LLLELNSCRP QEAARLVDEI
SAGERDGSLW PFMEAMFDCY GVDVEDHSRD CHILWPSENL RIAHFPMLQD DGLTVTINRD
IALAREDMQF LTAEHPMVLS AMDLVLSSET GNAAVSVIKH PQLKAGQFLL ELLFVAECSA
PAELQIGRFL PHTPLRVLVD QHKKDLTLVI SHDSLVETGD SFDKAQISQF LNSQRQHIQD
MIKVAEQLAG AQMQKLIAES SNLMIATLTG EIKRLVRLKK INPGIKEQEI EQLKEMTMLS
HESIQETQLR LDAVRFVITS
//
