ID   A0A223CZZ3_9BACL        Unreviewed;      1095 AA.
AC   A0A223CZZ3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN   ORFNames=CIG75_06715 {ECO:0000313|EMBL:ASS74694.1};
OS   Tumebacillus algifaecis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Tumebacillus.
OX   NCBI_TaxID=1214604 {ECO:0000313|EMBL:ASS74694.1, ECO:0000313|Proteomes:UP000214688};
RN   [1] {ECO:0000313|EMBL:ASS74694.1, ECO:0000313|Proteomes:UP000214688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=THMBR28 {ECO:0000313|EMBL:ASS74694.1,
RC   ECO:0000313|Proteomes:UP000214688};
RX   PubMed=25858243; DOI=10.1099/ijs.0.000240;
RA   Wu Y.F., Zhang B., Xing P., Wu Q.L., Liu S.J.;
RT   "Tumebacillus algifaecis sp. nov., isolated from decomposing algal scum.";
RL   Int. J. Syst. Evol. Microbiol. 65:2194-2198(2015).
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP022657; ASS74694.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A223CZZ3; -.
DR   KEGG; tab:CIG75_06715; -.
DR   OrthoDB; 2378884at2; -.
DR   Proteomes; UP000214688; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   CDD; cd05930; A_NRPS; 1.
DR   CDD; cd19531; LCL_NRPS-like; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.980; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   3: Inferred from homology;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000214688}.
FT   DOMAIN          989..1064
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          1070..1095
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1095 AA;  122633 MW;  9C4CAB9F7B275A3A CRC64;
     MFLLTDTKEE LQGTEEGVYL FPLSYAQQRL WFLDQFMPGN PAYNISTAVR LNGTLHSDQL
     LHALRQIAVR HETLCTSFRE VDGVAMQVID PSISLQLPLI DLSALSKEEQ QARVAAQITS
     QAQEPFDLKT APLLRLTLLK LSEVEHVLLL TMHHIISDGW SMNVLIYELS QLYNAALSGE
     EAVLPELVIQ YADFGDWQKE YLESGVLTEQ LSYWRDKLGG KLPILQLPAD HKRPAVQSYN
     GALETFLVPA RLADQLRTLS QGEGVSLFMT LLAAFKTLLF RYTGQQDQLV GTPIAGRTRE
     EIEPLIGFFV NTLVMRTELT EDMSFRTLLQ RVKDTAFEAY AHQDVPFEKL VEELAPERNI
     SHTPLFQVMF NLQNASVENL SLTGLTLEAL DADTGSSSFD LTLSMTEGKA GISGRIEYST
     DLFERTTIQR MIPHFLTLLE ALAGNPDLEL AALPLLTAEE RKLVIETFND TEADFRTDLC
     MHQMFELQVQ KTPDTVAVEH LEERITYAEL NARANQLAHY LQEMGIGPEK LVGLCMNRSI
     NLIIGLLGIL KAGGAFLPLD PDYPAERLRY LLNDSGVSVL LTESELLERL PEHSANVVCI
     DRDGDKIDSF ATENCESGVG PENLAYLIYT SGSTGAPKGA MLEHRNAVSH HYGVIDRYNV
     TASDRIVQFT SISFDVTVEE IFPTLATGAT LVLRPQKTLM ASDEFLAWLT EQRITKFNPP
     TAYVQTFLRD LAELKLSLPP TLRLMIAGGE RALPSMIRSW REVATEHNLL YNGYGPTETT
     VTATVYNEEL PDDDVPIGRP VANSQTYVLD VRLQPVPIGI PGELYIGGRN VGRGYLGRPD
     LTAERFVQNP FRVGERMYKT GDIVRFLPDG NLQFIGRADG QVKIRGYRIE LGEIENALSE
     APGVREAVVI DREDIPEQKY LAAYVTLQSA ELTAGDLRKH LAQRLPEYMI PSAFVIMDEM
     PMTPNGKVNR KELPRPDDDR PELGNAYIAP RTDLERSIAE IWQEVLGVSR VGIHDNFFEL
     GGGSLLILQV HRQLKENLGI ETSVVQLFQY PTVGTLAKFL GDDAEEISVK QGQDRADRRK
     DLKSRRAART KNRRE
//