ROCR_BACSU
ID ROCR_BACSU Reviewed; 461 AA.
AC P38022;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 29-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Transcriptional activator RocR;
DE AltName: Full=Arginine utilization regulatory protein RocR;
GN Name=rocR; OrderedLocusNames=BSU40350;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=8113162; DOI=10.1128/jb.176.5.1234-1241.1994;
RA Calogero S., Gardan R., Glaser P., Schweitzer J., Rapoport G.,
RA Debarbouille M.;
RT "RocR, a novel regulatory protein controlling arginine utilization in
RT Bacillus subtilis, belongs to the NtrC/NifA family of transcriptional
RT activators.";
RL J. Bacteriol. 176:1234-1241(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9205843; DOI=10.1093/dnares/4.2.155;
RA Kasahara Y., Nakai S., Ogasawara N.;
RT "Sequence analysis of the 36-kb region between gntZ and trnY genes of
RT Bacillus subtilis genome.";
RL DNA Res. 4:155-159(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP FUNCTION AS A REGULATOR, AND INDUCTION.
RC STRAIN=168;
RX PubMed=7540694; DOI=10.1006/jmbi.1995.0342;
RA Gardan R., Rapoport G., Debarbouille M.;
RT "Expression of the rocDEF operon involved in arginine catabolism in
RT Bacillus subtilis.";
RL J. Mol. Biol. 249:843-856(1995).
CC -!- FUNCTION: Positive regulator of arginine catabolism. Controls the
CC transcription of the two operons rocABC and rocDEF and probably acts by
CC binding to the corresponding upstream activating sequences.
CC {ECO:0000269|PubMed:7540694}.
CC -!- INDUCTION: Not induced by arginine, repressed by RocR itself.
CC {ECO:0000269|PubMed:7540694}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene do not grow in presence
CC of arginine as sole nitrogen source. {ECO:0000269|PubMed:8113162}.
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DR EMBL; L22006; AAA19792.1; -; Unassigned_DNA.
DR EMBL; D78193; BAA11294.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16072.1; -; Genomic_DNA.
DR PIR; A53370; A53370.
DR RefSeq; NP_391915.1; NC_000964.3.
DR RefSeq; WP_003244510.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P38022; -.
DR SMR; P38022; -.
DR STRING; 224308.BSU40350; -.
DR PaxDb; P38022; -.
DR PRIDE; P38022; -.
DR EnsemblBacteria; CAB16072; CAB16072; BSU_40350.
DR GeneID; 937769; -.
DR KEGG; bsu:BSU40350; -.
DR PATRIC; fig|224308.179.peg.4366; -.
DR eggNOG; COG3829; Bacteria.
DR InParanoid; P38022; -.
DR OMA; QAPIYIS; -.
DR PhylomeDB; P38022; -.
DR BioCyc; BSUB:BSU40350-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR GO; GO:0006525; P:arginine metabolic process; IDA:UniProtKB.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR002197; HTH_Fis.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR002078; Sigma_54_int.
DR InterPro; IPR025662; Sigma_54_int_dom_ATP-bd_1.
DR InterPro; IPR025943; Sigma_54_int_dom_ATP-bd_2.
DR InterPro; IPR025944; Sigma_54_int_dom_CS.
DR Pfam; PF02954; HTH_8; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00158; Sigma54_activat; 1.
DR PRINTS; PR01590; HTHFIS.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS00675; SIGMA54_INTERACT_1; 1.
DR PROSITE; PS00676; SIGMA54_INTERACT_2; 1.
DR PROSITE; PS00688; SIGMA54_INTERACT_3; 1.
DR PROSITE; PS50045; SIGMA54_INTERACT_4; 1.
PE 1: Evidence at protein level;
KW Activator; Arginine metabolism; ATP-binding; DNA-binding;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Two-component regulatory system.
FT CHAIN 1..461
FT /note="Transcriptional activator RocR"
FT /id="PRO_0000081218"
FT DOMAIN 143..372
FT /note="Sigma-54 factor interaction"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT DNA_BIND 434..453
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT BINDING 171..178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT BINDING 233..242
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00193"
FT MOD_RES 57
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000250"
FT CONFLICT 156..157
FT /note="NA -> KP (in Ref. 1; AAA19792)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 461 AA; 52177 MW; 58850E485E32C226 CRC64;
MVKDSEFLTL VFQSILDEID VGLHVVDEHG NTIVYNNKMM QIEDMEKHDV LNKNLMDVFM
FSKQQDSTLV QALQEGKTIK NVKQSYFNNK GQEITTINHT YPIVQDGKIR GAVEIAKDVT
KLERLIRENM NKKGSTTYTF DSILGTSPAI QDVIENAKRA TRTSSSVLLA GETGTGKELF
AQSIHNGSDR SGGPFISQNC AALPDSLVES ILFGTKKGAF TGAVDQPGLF EQAHGGTLLL
DEINSLNLSL QAKLLRALQE RKIRRIGSTK DTPIDVRIIA TMNEDPIDAI AGERMRKDLY
YRLSVVTLII PPLRERKEDI LLLASEFIQK NNHLFQMNVE HISDDVKQFF LSYDWPGNIR
ELEHMIEGAM NFMTDEQTIT ASHLPYQYRM KIKPADIPEP ETPRHQPAAD LKEKMESFEK
YVIENVLRKH GHNISKAAQE LGISRQSLQY RLKKFSHSSN E
