(data stored in ACNUC7421 zone)

SWISSPROT: A8FQ14_SHESH

ID   A8FQ14_SHESH            Unreviewed;        82 AA.
AC   A8FQ14;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   30-AUG-2017, entry version 75.
DE   RecName: Full=Acyl carrier protein {ECO:0000256|HAMAP-Rule:MF_01217};
DE            Short=ACP {ECO:0000256|HAMAP-Rule:MF_01217};
GN   Name=acpP {ECO:0000256|HAMAP-Rule:MF_01217};
GN   OrderedLocusNames=Ssed_0324 {ECO:0000313|EMBL:ABV34937.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34937.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34937.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34937.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01217}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01217}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01217}.
CC   -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific
CC       serine of apo-ACP by AcpS. This modification is essential for
CC       activity because fatty acids are bound in thioester linkage to the
CC       sulfhydryl of the prosthetic group. {ECO:0000256|HAMAP-
CC       Rule:MF_01217}.
CC   -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
CC       {ECO:0000256|HAMAP-Rule:MF_01217}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00258}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000821; ABV34937.1; -; Genomic_DNA.
DR   RefSeq; WP_012004463.1; NC_009831.1.
DR   ProteinModelPortal; A8FQ14; -.
DR   STRING; 425104.Ssed_0324; -.
DR   EnsemblBacteria; ABV34937; ABV34937; Ssed_0324.
DR   KEGG; sse:Ssed_0324; -.
DR   eggNOG; ENOG4105WBY; Bacteria.
DR   eggNOG; COG0236; LUCA.
DR   HOGENOM; HOG000178184; -.
DR   KO; K02078; -.
DR   OMA; DHIKRQT; -.
DR   OrthoDB; POG091H00VW; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000036; F:ACP phosphopantetheine attachment site binding involved in fatty acid biosynthetic process; IEA:UniProtKB-HAMAP.
DR   HAMAP; MF_01217; Acyl_carrier; 1.
DR   InterPro; IPR003231; Acyl_carrier.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   PROSITE; PS50075; ACP_DOMAIN; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FQ14.
DR   SWISS-2DPAGE; A8FQ14.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01217};
KW   Fatty acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01217};
KW   Fatty acid metabolism {ECO:0000256|HAMAP-Rule:MF_01217};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01217};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01217};
KW   Phosphopantetheine {ECO:0000256|HAMAP-Rule:MF_01217};
KW   Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01217}.
FT   DOMAIN        7     77       Carrier. {ECO:0000259|PROSITE:PS50075}.
FT   MOD_RES      40     40       O-(pantetheine 4'-phosphoryl)serine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01217}.
SQ   SEQUENCE   82 AA;  9223 MW;  09FFD6D2E0F87D2F CRC64;
     MQSREQILEA LTQILVDEFE IEAEDITLEA SLYQELDLDS IDAVDLVIKL QQMTGKKIKP
     EEFKAVRTVD DVVTAIEGLT KG
//

If you have problems or comments...

PBIL Back to PBIL home page