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
