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ACP_VIBHA
ID   ACP_VIBHA               Reviewed;          77 AA.
AC   P0A2W3; P55337; Q9R506;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 81.
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};
OS   Vibrio harveyi (Beneckea harveyi).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33843 / NCIMB 1871 / 392 / MAV;
RX   PubMed=8550484; DOI=10.1128/jb.178.2.571-573.1996;
RA   Shen Z., Byers D.M.;
RT   "Isolation of Vibrio harveyi acyl carrier protein and the fabG, acpP, and
RT   fabF genes involved in fatty acid biosynthesis.";
RL   J. Bacteriol. 178:571-573(1996).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-17.
RX   PubMed=8300523; DOI=10.1128/jb.176.3.681-690.1994;
RA   Heaton M.P., Neuhaus F.C.;
RT   "Role of the D-alanyl carrier protein in the biosynthesis of D-alanyl-
RT   lipoteichoic acid.";
RL   J. Bacteriol. 176:681-690(1994).
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; U39441; AAC43590.1; -; Genomic_DNA.
DR   PIR; T12052; T12052.
DR   RefSeq; WP_004406112.1; NZ_UAVF01000033.1.
DR   AlphaFoldDB; P0A2W3; -.
DR   SMR; P0A2W3; -.
DR   STRING; 669.AL538_03890; -.
DR   GeneID; 61874020; -.
DR   GeneID; 64085475; -.
DR   GeneID; 67376777; -.
DR   OrthoDB; 1943389at2; -.
DR   BRENDA; 2.7.8.7; 6632.
DR   UniPathway; UPA00094; -.
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   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.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..77
FT                   /note="Acyl carrier protein"
FT                   /id="PRO_0000180214"
FT   DOMAIN          2..77
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         37
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   77 AA;  8531 MW;  6639D3E77C789DEF CRC64;
     MSNIEERVKK IIVEQLGVDE AEVKNEASFV DDLGADSLDT VELVMALEEE FDTEIPDEEA
     EKITTVQAAI DYVNSAQ
 
 
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