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}.
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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
