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Database: UniProt
Entry: A0A223CXM5_9BACL
LinkDB: A0A223CXM5_9BACL
Original site: A0A223CXM5_9BACL 
ID   A0A223CXM5_9BACL        Unreviewed;      2314 AA.
AC   A0A223CXM5;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=Carrier domain-containing protein {ECO:0000259|PROSITE:PS50075};
GN   ORFNames=CIG75_03350 {ECO:0000313|EMBL:ASS74119.1};
OS   Tumebacillus algifaecis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Tumebacillus.
OX   NCBI_TaxID=1214604 {ECO:0000313|EMBL:ASS74119.1, ECO:0000313|Proteomes:UP000214688};
RN   [1] {ECO:0000313|EMBL:ASS74119.1, ECO:0000313|Proteomes:UP000214688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=THMBR28 {ECO:0000313|EMBL:ASS74119.1,
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}.
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DR   EMBL; CP022657; ASS74119.1; -; Genomic_DNA.
DR   KEGG; tab:CIG75_03350; -.
DR   OrthoDB; 9765680at2; -.
DR   Proteomes; UP000214688; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd05930; A_NRPS; 1.
DR   CDD; cd12117; A_NRPS_Srf_like; 1.
DR   CDD; cd19531; LCL_NRPS-like; 2.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 3.40.50.980; -; 4.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 3.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR029058; AB_hydrolase.
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   InterPro; IPR006162; Ppantetheine_attach_site.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 2.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF13193; AMP-binding_C; 2.
DR   Pfam; PF00668; Condensation; 3.
DR   Pfam; PF00550; PP-binding; 2.
DR   SMART; SM00823; PKS_PP; 2.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 5.
DR   PROSITE; PS00455; AMP_BINDING; 2.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000214688}.
FT   DOMAIN          995..1070
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          2051..2126
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          2141..2178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2162..2178
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2314 AA;  258279 MW;  0DC96BF5DBB750CD CRC64;
     MADELTKQGE LLLEADGEEI EYYEFPASFA QNRMWLINQM NESSGMYNMP MAVRFEGPLH
     IEALEKSLQE IVERHETLRT TFAMEDGELF QLIASQAKVK IPLLDLTSLS KAEQQAKVEA
     LSSLEAETPF DLEEGPLLRS TLLKLGEQEH VLLFAKHHII SDGMSMAVMI HELVMLYEAF
     IDGKPSPLPP LEIQYADFAA WQRDWFTGSV YEKHIDYWRG QLGGSIAPLQ LPTDRARPAV
     ASPEGGHVLL PLPDSLMEQV NALTKQFKGS TLFMTMLAAY KAFLYRYTGQ DDLAVGTPIA
     GRKQPGIEHL IGFFVNTLVL RTDLSDDPTF RELLERVRRV TLDAYTYQEM PFEKLVEELQ
     PDRSVSNPFF QTMFVVQNVS TPDLTLRDLK ISAVEVQRNT AKFDLMFTVD QKDGKPILFA
     EYSTDLFDYE TVERMMGHYL NLLQAVVDNP DLPISQLSML TEAEIHTLTV DCNQTERDFP
     TDRLVHELFE QRAADNPDAI AIQYEEEQVT YRELNERANQ LARLLKGEGV GPEKVVGIYL
     ERSPNMIVAL LAILKAGGAF VAFDPAFPQD RIGFMMEDSE VPVILTQQSL AGLLPQHEAK
     TFCLDAQWDE VAGNGTDNLP NEATLQNLVY LIFTSGSTGR SKGVQVEHRN LLNYLYAIEE
     VAQLGDGASY GNVSTLSADV GHTAIFPALC RGGTLHIIAQ ERLTDPDLMA EYFEKHPVDC
     LKIVPTHLAA LMASQPLKVL PKHGAVVGGE TLRWDMIERV EQYRDDVWLI NHYGPTEVTI
     AGVVYKVEKD PAMRQTVTVP LGRPLGNVQV YVLDKHLHPV PYGVAGEVYF GGAGITRGYI
     KRPDLTAERY LKDPFKSDPD ARFYRTGDLA KRHPDGRLEF LTRADTQVKI RGYRVELGEV
     ETVIGQHELV KENVVVARED VPGDRRLVAY IVKNEGVEGG TTDVRNYLKE ILPDYMIPAV
     FVYLDAIPLT ANGKIDRRIL PDPEAELMEQ SEYIAPSTEL EAKVAQIWAE VLHVEQVSVV
     DNFFDLGGHS LMVTQVVSRV NKEFAIKIPL RTLFEAPTVV DLALRVEAQM QETLAPTASE
     APIKPVARDT KLPLSFSQQR LWVLEQLIPG LTAYNIPYAV RLTGALHNEH FERALNMMIE
     RHESFRTTFS DASGEPEQLI HEAVWTPLQL VDLQHLSGTE QEAEVARLVR AENDTPFDLR
     KGPLIRNQLL KLGEQEHVLL LTLHHIISDG WSRGILTKEL THLYDVLVTG KESALSPLPL
     QYADFAVWQR EFLEQELGSQ LSYWKEKLGQ DLPVLQLPTD RPRPPMQTHN GAQLTFRLPQ
     KVGDQLTALS QKQGATLFMT LLAAFQTLIL HYSGQEDFAV GTPIANRNRQ DTESIIGFFV
     NTLALRADLS GNPTFLELIG RAKDAALGAY ANQDVPFEKI VEELETDRDL SRSPVFQVVF
     GLQNFEQSKI ELAGLTFEPV ADTGTTSKFD LSLLMSEHED QSIGGTFEYN SDLFEASTIE
     RMLHQFVQLT AALVENPAQR VGELSLLTTA EREQLVVEWN RTASAYPGAS LQELFEAQAA
     AIPDAVAVVS GNDSLTYRQL NERANQIAHH LKALGVGPDA LVGLCIERSL EMVTALLAII
     KAGGGYVPID SDYPQERIAF MLEDTNVSVL VTQSALAEKL PLPDSHVICL DRDMQLFADQ
     STDNPNCATT QDNLAYVIYT SGSTGRPKGV LVPQRGVVRL VKNTNYMQMT ADQVFLQTAS
     LSFDAATFEI WGPLLNGAKL ALMPVGQSSL EDLGRLVKTY GVTVLWLSAG LFHQMVEFRL
     DDLQGVKYLL SGGDVLSVAH VKKALDNLSG LTIINCYGPT ENTSFTTVHA MTDVAQVGNT
     VSIGGPISNT TVYVLNQHLQ PVPVGVPGEL LTGGDGLAVG YLNRPDLTQE KFVETAFGRL
     YKTGDLVRWL SDGTLEFMGR IDQQVKIRGF RIEIGEIETL LSNLPGVRAC TVIAHEADGD
     KRLVGYVVPE PGEQVQVEEL RTLLRKQLPD YMMPSFLVLL DELPLTSNGK VDRKRLPSPE
     GTLSDRDDYV APRTEEEQKV AQIFANVLRV EKVGMHDNFF ALGGHSLLAT QVVSRIAEEY
     GVAVPLRLLF QFPTVAEFTA ELLRARAEGT VQTTGAMEIQ RVSRRSEVPE ISAVPRRRGG
     SPRSADAQRA EEPKHTGEPY VHPLREAVRL DLMERAQYEL FAAHDVLRTL LHGTEDELVK
     QVKDAKWSPL HVIYLRDLEE QALEAKLQEL LQTERQKPLE PQSETVRFYL IQKGASDFVF
     VLNLHPLLAK EVSAAELVKE LLTKYQSYLQ ELAQ
//
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