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ACP_SYNY3
ID   ACP_SYNY3               Reviewed;          77 AA.
AC   P20804; P73284;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-MAY-2022, entry version 143.
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}; Synonyms=acp;
GN   OrderedLocusNames=ssl2084;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-61, AND NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-45.
RC   STRAIN=ATCC 27184;
RX   PubMed=2123456; DOI=10.1111/j.1432-1033.1990.tb19405.x;
RA   Froehlich J.E., Poorman R., Reardon E., Barnum S.R., Jaworski J.G.;
RT   "Purification and characterization of acyl carrier protein from two
RT   cyanobacteria species.";
RL   Eur. J. Biochem. 193:817-825(1990).
CC   -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid
CC       biosynthesis.
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.
CC   -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
CC       {ECO:0000255|HAMAP-Rule:MF_01217}.
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DR   EMBL; BA000022; BAA17312.1; -; Genomic_DNA.
DR   PIR; S77465; S77465.
DR   AlphaFoldDB; P20804; -.
DR   SMR; P20804; -.
DR   IntAct; P20804; 2.
DR   STRING; 1148.1652390; -.
DR   PaxDb; P20804; -.
DR   EnsemblBacteria; BAA17312; BAA17312; BAA17312.
DR   KEGG; syn:ssl2084; -.
DR   eggNOG; COG0236; Bacteria.
DR   InParanoid; P20804; -.
DR   OMA; CEIPDEQ; -.
DR   PhylomeDB; P20804; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0000035; F:acyl binding; IBA:GO_Central.
DR   GO; GO:0000036; F:acyl carrier activity; IBA:GO_Central.
DR   GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central.
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   InterPro; IPR006162; Ppantetheine_attach_site.
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.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Lipid biosynthesis; Lipid metabolism;
KW   Phosphopantetheine; Phosphoprotein; Reference proteome.
FT   CHAIN           1..77
FT                   /note="Acyl carrier protein"
FT                   /id="PRO_0000180207"
FT   DOMAIN          3..77
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         38
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   CONFLICT        2
FT                   /note="N -> D (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        23
FT                   /note="K -> G (in Ref. 2; AA sequence)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   77 AA;  8590 MW;  FDDED4DBFD6EBD53 CRC64;
     MNQEIFEKVK KIVVEQLEVD PDKVTPDATF AEDLGADSLD TVELVMALEE EFDIEIPDEV
     AETIDTVGKA VEHIESK
 
 
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