ACP_AZOBR
ID ACP_AZOBR Reviewed; 79 AA.
AC P94123;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 102.
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}; Synonyms=acpF;
OS Azospirillum brasilense.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=RG;
RX PubMed=8760922; DOI=10.1099/13500872-142-8-2097;
RA Maiti M.K., Ghosh S.;
RT "Acyl carrier protein of Azospirillum brasilense: properties of the
RT purified protein and sequencing of the corresponding gene, acpP.";
RL Microbiology 142:2097-2103(1996).
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; X82399; CAA57794.1; -; Genomic_DNA.
DR RefSeq; WP_014240383.1; NZ_WFKD01000127.1.
DR AlphaFoldDB; P94123; -.
DR SMR; P94123; -.
DR GeneID; 56448189; -.
DR OrthoDB; 1943389at2; -.
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 CHAIN 2..79
FT /note="Acyl carrier protein"
FT /id="PRO_0000180095"
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 79 AA; 8544 MW; A87A4C7AEBF16F6C CRC64;
MSDVAERVKK IVVDHLGVEE SKVTENASFI DDLGADSLDT VELVMAFEEE FGCEIPDDAA
EKILTVKDAI DFIKANAAA