ID   ACP_BRAHO               Reviewed;          78 AA.
AC   O34163;
DT   02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Acyl carrier protein;
DE            Short=ACP;
DE   Contains:
DE     RecName: Full=Beta-hemolysin;
GN   Name=acpP; Synonyms=hlyA;
OS   Brachyspira hyodysenteriae (Treponema hyodysenteriae).
OC   Bacteria; Spirochaetes; Brachyspirales; Brachyspiraceae; Brachyspira.
OX   NCBI_TaxID=159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 8-20, AND FUNCTION.
RC   STRAIN=B204;
RX   PubMed=11159958; DOI=10.1128/iai.69.2.706-711.2001;
RA   Hsu T., Hutto D.L., Minion F.C., Zuerner R.L., Wannemuehler M.J.;
RT   "Cloning of a beta-hemolysin gene of Brachyspira (Serpulina) hyodysenteriae
RT   and its expression in Escherichia coli.";
RL   Infect. Immun. 69:706-711(2001).
CC   -!- FUNCTION: Carrier of the growing fatty acid chain in fatty acid
CC       biosynthesis (By similarity). Has hemolytic activity forming pores
CC       approximately 1 nm in diameter into erythrocytes. Is able to induce
CC       murine colonic lesions and to disrupt the integrity of epithelial cell
CC       monolayers. {ECO:0000250, ECO:0000269|PubMed:11159958}.
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Secreted.
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 (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
CC       {ECO:0000305}.
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DR   EMBL; U94886; AAB68774.1; -; Genomic_DNA.
DR   RefSeq; WP_008724300.1; NZ_MKXF01000041.1.
DR   AlphaFoldDB; O34163; -.
DR   SMR; O34163; -.
DR   GeneID; 63963776; -.
DR   GeneID; 66488063; -.
DR   UniPathway; UPA00094; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-UniRule.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0000036; F:acyl carrier activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
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   Cytolysis; Direct protein sequencing; Fatty acid biosynthesis;
KW   Fatty acid metabolism; Hemolysis; Lipid biosynthesis; Lipid metabolism;
KW   Phosphopantetheine; Phosphoprotein; Secreted; Toxin; Virulence.
FT   CHAIN           1..78
FT                   /note="Acyl carrier protein"
FT                   /id="PRO_0000225621"
FT   CHAIN           8..78
FT                   /note="Beta-hemolysin"
FT                   /id="PRO_0000000560"
FT   DOMAIN          1..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;  8934 MW;  5F21E7ED0102C715 CRC64;
     MALIDEIKDV VANQLNISDK SKITDTASFV DDLNADSLDL VELIMELEKR YEIKIPQEDQ
     EKIKNVADAA KYIEEHKK