ACP_MORMI
ID ACP_MORMI Reviewed; 78 AA.
AC Q9RA32;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 90.
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 Moritella marina (Vibrio marinus).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Moritellaceae; Moritella.
OX NCBI_TaxID=90736;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 15381 / BCRC 15891 / CIP 102861 / NCIMB 1144 / MP-1;
RA Morita N., Ueno A., Tamaka M., Ohgiya S., Hoshino T., Kawasaki K.,
RA Yumoto I., Ishizaki K., Okuyama H.;
RT "Cloning and sequencing of clustered genes involved in fatty acid
RT biosynthesis from the docosahexaenoic acid-producing bacterium, Vibrio
RT marinus strain MP-1.";
RL Biotechnol. Lett. 21:641-646(1999).
CC -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid
CC biosynthesis (By similarity). Is probably involved in the biosynthesis
CC of docosahexaenoic acid (DHA) which is produced by this bacterium as a
CC fatty acyl component in its membrane lipid. {ECO:0000255|HAMAP-
CC 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; AB021978; BAA85257.1; -; Genomic_DNA.
DR PIR; T44435; T44435.
DR AlphaFoldDB; Q9RA32; -.
DR SMR; Q9RA32; -.
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 3: Inferred from homology;
KW Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Phosphopantetheine; Phosphoprotein.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..78
FT /note="Acyl carrier protein"
FT /id="PRO_0000180215"
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 78 AA; 8696 MW; E19BBAD31AAD6861 CRC64;
MSNFEERVKK IIIEQLGVKE EEVKNEASFV DDLGADSLDT VELVMALEEE FDTDIPDDEA
EKITTVQAAI DYVVSSAE
