位置:首页 > 蛋白库 > ACP_RICPR
ACP_RICPR
ID   ACP_RICPR               Reviewed;          86 AA.
AC   Q9ZCH9;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 114.
DE   RecName: Full=Acyl carrier protein {ECO:0000255|HAMAP-Rule:MF_01217};
DE            Short=ACP {ECO:0000255|HAMAP-Rule:MF_01217};
GN   Name=acpP {ECO:0000255|HAMAP-Rule:MF_01217}; OrderedLocusNames=RP763;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
CC   -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid
CC       biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01217}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000255|HAMAP-
CC       Rule:MF_01217}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01217}.
CC   -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC       of apo-ACP by AcpS. This modification is essential for activity because
CC       fatty acids are bound in thioester linkage to the sulfhydryl of the
CC       prosthetic group. {ECO:0000255|HAMAP-Rule:MF_01217}.
CC   -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
CC       {ECO:0000255|HAMAP-Rule:MF_01217}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ235273; CAA15191.1; -; Genomic_DNA.
DR   PIR; G71636; G71636.
DR   RefSeq; NP_221115.2; NC_000963.1.
DR   PDB; 2LOL; NMR; -; A=6-86.
DR   PDBsum; 2LOL; -.
DR   AlphaFoldDB; Q9ZCH9; -.
DR   SMR; Q9ZCH9; -.
DR   STRING; 272947.RP763; -.
DR   EnsemblBacteria; CAA15191; CAA15191; CAA15191.
DR   KEGG; rpr:RP763; -.
DR   PATRIC; fig|272947.5.peg.799; -.
DR   eggNOG; COG0236; Bacteria.
DR   HOGENOM; CLU_108696_5_6_5; -.
DR   OMA; CEIPDEQ; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000002480; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   HAMAP; MF_01217; Acyl_carrier; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR003231; Acyl_carrier.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   PANTHER; PTHR20863; PTHR20863; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   TIGRFAMs; TIGR00517; acyl_carrier; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW   Lipid biosynthesis; Lipid metabolism; Phosphopantetheine; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN           1..86
FT                   /note="Acyl carrier protein"
FT                   /id="PRO_0000180180"
FT   DOMAIN          10..85
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         45
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   HELIX           9..23
FT                   /evidence="ECO:0007829|PDB:2LOL"
FT   TURN            28..30
FT                   /evidence="ECO:0007829|PDB:2LOL"
FT   HELIX           37..40
FT                   /evidence="ECO:0007829|PDB:2LOL"
FT   HELIX           45..59
FT                   /evidence="ECO:0007829|PDB:2LOL"
FT   HELIX           65..70
FT                   /evidence="ECO:0007829|PDB:2LOL"
FT   STRAND          71..73
FT                   /evidence="ECO:0007829|PDB:2LOL"
FT   HELIX           74..84
FT                   /evidence="ECO:0007829|PDB:2LOL"
SQ   SEQUENCE   86 AA;  9887 MW;  906C044E4DFE8E4F CRC64;
     MEFKIMSTTD KIEQKVIEMV AEKLNKDKAI ITTDSRFIED LKADSLDTVE LMMAIEVEYG
     IDIPDDEATK IKTVSDVIKY IKERQS
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024