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Database: UniProt
Entry: E1V9P9_HALED
LinkDB: E1V9P9_HALED
Original site: E1V9P9_HALED 
ID   E1V9P9_HALED            Unreviewed;        77 AA.
AC   E1V9P9;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 81.
DE   RecName: Full=Acyl carrier protein {ECO:0000256|HAMAP-Rule:MF_01217, ECO:0000256|RuleBase:RU003545};
DE            Short=ACP {ECO:0000256|HAMAP-Rule:MF_01217};
GN   Name=acpP {ECO:0000256|HAMAP-Rule:MF_01217,
GN   ECO:0000313|EMBL:CBV41883.1};
GN   OrderedLocusNames=HELO_1999 {ECO:0000313|EMBL:CBV41883.1};
OS   Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS   / 1H9).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=768066 {ECO:0000313|EMBL:CBV41883.1, ECO:0000313|Proteomes:UP000008707};
RN   [1] {ECO:0000313|Proteomes:UP000008707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9
RC   {ECO:0000313|Proteomes:UP000008707};
RX   PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA   Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA   Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA   Kunte H.J.;
RT   "A blueprint of ectoine metabolism from the genome of the industrial
RT   producer Halomonas elongata DSM 2581(T).";
RL   Environ. Microbiol. 13:1973-1994(2011).
CC   -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid
CC       biosynthesis. {ECO:0000256|HAMAP-Rule:MF_01217,
CC       ECO:0000256|RuleBase:RU003545}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis. {ECO:0000256|HAMAP-
CC       Rule:MF_01217, ECO:0000256|RuleBase:RU003545}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_01217}.
CC   -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC       of apo-ACP by acpS. {ECO:0000256|RuleBase:RU003545}.
CC   -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
CC       {ECO:0000256|HAMAP-Rule:MF_01217}.
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DR   EMBL; FN869568; CBV41883.1; -; Genomic_DNA.
DR   RefSeq; WP_013331755.1; NC_014532.2.
DR   AlphaFoldDB; E1V9P9; -.
DR   STRING; 768066.HELO_1999; -.
DR   KEGG; hel:HELO_1999; -.
DR   eggNOG; COG0236; Bacteria.
DR   HOGENOM; CLU_108696_5_1_6; -.
DR   OrthoDB; 9804551at2; -.
DR   UniPathway; UPA00094; -.
DR   UniPathway; UPA00360; -.
DR   Proteomes; UP000008707; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0036104; P:Kdo2-lipid A biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   HAMAP; MF_01217; Acyl_carrier; 1.
DR   InterPro; IPR003231; ACP.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   NCBIfam; TIGR00517; acyl_carrier; 1.
DR   PANTHER; PTHR20863; ACYL CARRIER PROTEIN; 1.
DR   PANTHER; PTHR20863:SF77; ACYL CARRIER PROTEIN; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01217};
KW   Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160, ECO:0000256|HAMAP-
KW   Rule:MF_01217};
KW   Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832, ECO:0000256|HAMAP-
KW   Rule:MF_01217};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_01217};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_01217};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450, ECO:0000256|HAMAP-
KW   Rule:MF_01217};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|HAMAP-
KW   Rule:MF_01217}.
FT   DOMAIN          2..77
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   MOD_RES         37
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01217"
SQ   SEQUENCE   77 AA;  8689 MW;  71C407A6E107385C CRC64;
     MSTIEERVKK VVAERLNVKE EDIQSSSSFT EDLGADSLDT VELVMALEEE FDTEIPDEEA
     EKITTVQEAI DYVNAHQ
//
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