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URED_RHIME
ID   URED_RHIME              Reviewed;         277 AA.
AC   P42888;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 3.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Urease accessory protein UreD {ECO:0000255|HAMAP-Rule:MF_01384};
GN   Name=ureD {ECO:0000255|HAMAP-Rule:MF_01384}; OrderedLocusNames=R02476;
GN   ORFNames=SMc01942;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=AK631;
RX   PubMed=7813887; DOI=10.1016/0378-1097(94)90247-x;
RA   Miksch G.;
RT   "The urease structural gene ureA in Rhizobium meliloti is preceded by an
RT   open reading frame necessary for urease activity.";
RL   FEMS Microbiol. Lett. 124:185-190(1994).
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 168-277.
RC   STRAIN=AK631;
RX   PubMed=8121412; DOI=10.1007/bf00285277;
RA   Miksch G., Arnold W., Lentzsch P., Priefer U.B., Puehler A.;
RT   "A 4.6 kb DNA region of Rhizobium meliloti involved in determining urease
RT   and hydrogenase activities carries the structural genes for urease (ureA,
RT   ureB, ureC) interrupted by other open reading frames.";
RL   Mol. Gen. Genet. 242:539-550(1994).
CC   -!- FUNCTION: Required for maturation of urease via the functional
CC       incorporation of the urease nickel metallocenter. {ECO:0000255|HAMAP-
CC       Rule:MF_01384}.
CC   -!- SUBUNIT: UreD, UreF and UreG form a complex that acts as a GTP-
CC       hydrolysis-dependent molecular chaperone, activating the urease
CC       apoprotein by helping to assemble the nickel containing metallocenter
CC       of UreC. The UreE protein probably delivers the nickel.
CC       {ECO:0000255|HAMAP-Rule:MF_01384}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01384}.
CC   -!- SIMILARITY: Belongs to the UreD family. {ECO:0000255|HAMAP-
CC       Rule:MF_01384}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB33024.2; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; S76260; AAB33024.2; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL591688; CAC47055.1; -; Genomic_DNA.
DR   EMBL; S69145; AAB30133.1; -; Genomic_DNA.
DR   PIR; S42601; S42601.
DR   RefSeq; NP_386582.1; NC_003047.1.
DR   RefSeq; WP_010969965.1; NC_003047.1.
DR   AlphaFoldDB; P42888; -.
DR   SMR; P42888; -.
DR   STRING; 266834.SMc01942; -.
DR   EnsemblBacteria; CAC47055; CAC47055; SMc01942.
DR   GeneID; 61603935; -.
DR   KEGG; sme:SMc01942; -.
DR   PATRIC; fig|266834.11.peg.3965; -.
DR   eggNOG; COG0829; Bacteria.
DR   HOGENOM; CLU_056339_2_0_5; -.
DR   OMA; MARFCAQ; -.
DR   Proteomes; UP000001976; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   HAMAP; MF_01384; UreD; 1.
DR   InterPro; IPR002669; UreD.
DR   PANTHER; PTHR33643; PTHR33643; 1.
DR   Pfam; PF01774; UreD; 1.
PE   3: Inferred from homology;
KW   Chaperone; Cytoplasm; Nickel insertion; Reference proteome.
FT   CHAIN           1..277
FT                   /note="Urease accessory protein UreD"
FT                   /id="PRO_0000067614"
FT   CONFLICT        37
FT                   /note="C -> S (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        97..103
FT                   /note="AEIATRI -> PRLRRRV (in Ref. 1; AAB33024)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        171
FT                   /note="G -> A (in Ref. 1; AAB33024/AAB30133)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        181
FT                   /note="A -> S (in Ref. 1; AAB33024)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   277 AA;  29366 MW;  F800A62163D7C9C0 CRC64;
     MEPAAIIAPQ RARGEGRLVA KAEGGRTRIA ELYQEGCAKI RLPKTFDASM EAVLINSSGG
     VTGGDRLSWE FRAGKGTKLT LTTQACEKVY KAAAGTAEIA TRISVAAGAH VDWLPQETIL
     FDRSALSRSL EVDLAADASF LAVEAVLIGR KAMGEEVRAG LFRDNWRIRS GGRLIHAENL
     ALAGDIAALA SRRAVLDGAA AFATLVYAAP DCESQLSKLR LALAGHALSG VSHYDVGGRD
     KIVARVAAAD GFALRKILIP LISHLRKDAS VPKVWTL
 
 
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