ID F8E7A0_FLESM Unreviewed; 78 AA.
AC F8E7A0;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 75.
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 OrderedLocusNames=Flexsi_0119 {ECO:0000313|EMBL:AEI13815.1};
OS Flexistipes sinusarabici (strain ATCC 49648 / DSM 4947 / MAS 10).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Flexistipitaceae; Flexistipes.
OX NCBI_TaxID=717231 {ECO:0000313|EMBL:AEI13815.1, ECO:0000313|Proteomes:UP000006621};
RN [1] {ECO:0000313|EMBL:AEI13815.1, ECO:0000313|Proteomes:UP000006621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4947 / MAS 10 {ECO:0000313|Proteomes:UP000006621};
RX PubMed=22180813; DOI=10.4056/sigs.2235024;
RA Lapidus A., Chertkov O., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Rohde M.,
RA Abt B., Spring S., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Woyke T.;
RT "Genome sequence of the moderately thermophilic halophile Flexistipes
RT sinusarabici strain (MAS10).";
RL Stand. Genomic Sci. 5:86-96(2011).
RN [2] {ECO:0000313|Proteomes:UP000006621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4947 / MAS 10 {ECO:0000313|Proteomes:UP000006621};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Flexistipes sinusarabici DSM 4947.";
RL Submitted (JUN-2011) 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 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; CP002858; AEI13815.1; -; Genomic_DNA.
DR RefSeq; WP_013885329.1; NC_015672.1.
DR AlphaFoldDB; F8E7A0; -.
DR STRING; 717231.Flexsi_0119; -.
DR KEGG; fsi:Flexsi_0119; -.
DR eggNOG; COG0236; Bacteria.
DR HOGENOM; CLU_108696_5_1_0; -.
DR OrthoDB; 9804551at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000006621; Chromosome.
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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000006621}.
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 78 AA; 8841 MW; 17A0B2E4B58B322C CRC64;
MADVDAKVKE IIAEQLNIDE EEVKPEASFI DDLGADSLDT VELIMAFEEE FDLEIPDEEA
EKIKTVQDAV EHIKKHVQ
//
