ACP_CAMC1
ID ACP_CAMC1 Reviewed; 77 AA.
AC A7ZF37;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 79.
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};
GN OrderedLocusNames=Ccon26_15490; ORFNames=CCC13826_0561;
OS Campylobacter concisus (strain 13826).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360104;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13826;
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., On S., Nelson K.E.;
RT "Genome sequence of Campylobacter concisus 13826 isolated from human
RT feces.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid
CC biosynthesis. {ECO:0000255|HAMAP-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; CP000792; EAT99180.1; -; Genomic_DNA.
DR RefSeq; WP_002941395.1; NC_009802.2.
DR AlphaFoldDB; A7ZF37; -.
DR SMR; A7ZF37; -.
DR STRING; 360104.CCC13826_0561; -.
DR EnsemblBacteria; EAT99180; EAT99180; CCC13826_0561.
DR KEGG; cco:CCC13826_0561; -.
DR eggNOG; COG0236; Bacteria.
DR HOGENOM; CLU_108696_5_1_7; -.
DR OMA; CEIPDEQ; -.
DR OrthoDB; 1943389at2; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000001121; 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; -; 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 CHAIN 1..77
FT /note="Acyl carrier protein"
FT /id="PRO_1000073121"
FT DOMAIN 1..76
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 36
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 77 AA; 8590 MW; 6F95440CCAFA3055 CRC64;
MAVFEDVRDV VVEQLSVDPQ AVKLESKIIE DLGADSLDVV ELVMALEEKF EVEIPDSEAE
KLVSIQDVVN YIEKLGK