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DBH_RHIME
ID   DBH_RHIME               Reviewed;          90 AA.
AC   P02344;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 2.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=DNA-binding protein HRm;
GN   Name=hupB; OrderedLocusNames=R01258; ORFNames=SMc01906;
OS   Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS   meliloti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=266834;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=6299736; DOI=10.1111/j.1432-1033.1983.tb07265.x;
RA   Laine B., Belaiche D., Khanaka H., Sautiere P.;
RT   "Primary structure of the DNA-binding protein HRm from Rhizobium
RT   meliloti.";
RL   Eur. J. Biochem. 131:325-331(1983).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10762258; DOI=10.1128/jb.182.9.2551-2558.2000;
RA   Summers M.L., Botero L.M., Busse S.C., McDermott T.R.;
RT   "The Sinorhizobium meliloti lon protease is involved in regulating
RT   exopolysaccharide synthesis and is required for nodulation of alfalfa.";
RL   J. Bacteriol. 182:2551-2558(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11481430; DOI=10.1073/pnas.161294398;
RA   Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA   Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA   Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA   Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA   Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT   "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT   meliloti strain 1021.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1021;
RX   PubMed=11474104; DOI=10.1126/science.1060966;
RA   Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA   Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA   Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA   Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA   Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA   Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA   Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA   Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA   Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA   Wong K., Yeh K.-C., Batut J.;
RT   "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL   Science 293:668-672(2001).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-54.
RC   STRAIN=STR 3;
RX   PubMed=7049166; DOI=10.1016/0006-291x(82)92063-0;
RA   Laine B., Belaiche D., Sautiere P., Biserte G.;
RT   "Characterization and structural study of the DNA-binding protein HRm From
RT   Rhizobium meliloti.";
RL   Biochem. Biophys. Res. Commun. 106:101-107(1982).
CC   -!- FUNCTION: Histone-like DNA-binding protein which is capable of wrapping
CC       DNA to stabilize it, and thus to prevent its denaturation under extreme
CC       environmental conditions.
CC   -!- SIMILARITY: Belongs to the bacterial histone-like protein family.
CC       {ECO:0000305}.
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DR   EMBL; AF167159; AAF05301.1; -; Genomic_DNA.
DR   EMBL; AL591688; CAC45837.1; -; Genomic_DNA.
DR   PIR; S00053; DNZRHM.
DR   RefSeq; NP_385364.1; NC_003047.1.
DR   AlphaFoldDB; P02344; -.
DR   SMR; P02344; -.
DR   STRING; 266834.SMc01906; -.
DR   EnsemblBacteria; CAC45837; CAC45837; SMc01906.
DR   KEGG; sme:SMc01906; -.
DR   PATRIC; fig|266834.11.peg.2672; -.
DR   eggNOG; COG0776; Bacteria.
DR   HOGENOM; CLU_105066_3_2_5; -.
DR   OMA; PAHEGIN; -.
DR   Proteomes; UP000001976; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR   Gene3D; 4.10.520.10; -; 1.
DR   InterPro; IPR000119; Hist_DNA-bd.
DR   InterPro; IPR020816; Histone-like_DNA-bd_CS.
DR   InterPro; IPR010992; IHF-like_DNA-bd_dom_sf.
DR   PANTHER; PTHR33175; PTHR33175; 1.
DR   Pfam; PF00216; Bac_DNA_binding; 1.
DR   PRINTS; PR01727; DNABINDINGHU.
DR   SMART; SM00411; BHL; 1.
DR   SUPFAM; SSF47729; SSF47729; 1.
DR   PROSITE; PS00045; HISTONE_LIKE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; DNA condensation; DNA-binding;
KW   Reference proteome.
FT   CHAIN           1..90
FT                   /note="DNA-binding protein HRm"
FT                   /id="PRO_0000104962"
FT   CONFLICT        55
FT                   /note="Missing (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        61
FT                   /note="R -> RR (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   90 AA;  9303 MW;  C9B19D281DF5C2A5 CRC64;
     MNKNELVAAV ADKAGLSKAD ASSAVDAVFE TIQGELKNGG DIRLVGFGNF SVSRREASKG
     RNPSTGAEVD IPARNVPKFT AGKGLKDAVN
 
 
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