ID Q0BVN1_GRABC Unreviewed; 1321 AA.
AC Q0BVN1;
DT 17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 17-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE SubName: Full=Non-ribosomal peptide synthetase module {ECO:0000313|EMBL:ABI61121.1};
DE EC=6.3.2.- {ECO:0000313|EMBL:ABI61121.1};
GN OrderedLocusNames=GbCGDNIH1_0223 {ECO:0000313|EMBL:ABI61121.1};
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165 {ECO:0000313|EMBL:ABI61121.1, ECO:0000313|Proteomes:UP000001963};
RN [1] {ECO:0000313|EMBL:ABI61121.1, ECO:0000313|Proteomes:UP000001963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1 {ECO:0000313|Proteomes:UP000001963};
RX PubMed=17827295; DOI=10.1128/JB.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA Kupko J.J.III., Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(2007).
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DR EMBL; CP000394; ABI61121.1; -; Genomic_DNA.
DR STRING; 391165.GbCGDNIH1_0223; -.
DR KEGG; gbe:GbCGDNIH1_0223; -.
DR eggNOG; COG0110; Bacteria.
DR eggNOG; COG0663; Bacteria.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_002751_0_0_5; -.
DR OrthoDB; 9770470at2; -.
DR Proteomes; UP000001963; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 3.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
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; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR012728; NRPS_C.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR NCBIfam; TIGR02353; NRPS_term_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; PF00550; PP-binding; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 3.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Ligase {ECO:0000313|EMBL:ABI61121.1}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001963};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 664..689
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 855..878
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 898..924
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1110..1132
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1138..1163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 524..601
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1321 AA; 143073 MW; 043322D22DB4BCFF CRC64;
MNDMRDILAP VTPDHGSLAD VFRVTAARLP EKIAIRFRGQ AISYAELDAL SSRWAAVLAA
RGIGPGRFVG IWITRSIALH AAILAVLKTG AAYLPFDPEA PRERVDISVE DCQAAAVLVD
AAHLTLADGL SVPAITTDTL DETAPAIAPG ADAFQPPASN DPAYAIYTSG STGKPKGIAV
CQSNIRHLLH SENAVLGIRE DDIVYQGFSP AFDMSLEEVF ISYLAGATLI VAPPELVRAS
DALPDVLTEE NVTVLHCVPT LLAMLDRDVP SLRLINMGGE ACPAALVDRW WKPGRRLLNT
YGPTETTVTA TAAELEPGDP ITIGYPLPGY TAYILDETTL APVPAGEGGE LLIGGPGVSL
GYIGRPELTA EKFIRNPLVA ADASDIPDPV LYRTGDKASF DTEGRIVFHG RIDDQIKFRG
YRIETGEIEA ELGKLDAVRA AAVVLREDSA GTQHLVAFIS YAEGATPDAG TIRTALAARL
PAYMLPTVFL ALDEIPRLPS GKINRKALPA VIETIAPEKR DIVAPRNPAE AALVEAAQAV
FPHIQVSTID DFFQDLGGHS LSAAGLVSRL RQDERFRSVS IQDLYECRTL DRLAAKFADT
ATGDTEAVLP PFQTVPPWRH RLCGAAQSVA LIPIFGLQAI RDIVPYLVFS ALMEFDWTLR
QAILGTLLTF VLTPLVITAI AIAAKWLVIG RYKPGSYPLW GSYYFRWWFV SRMLQVVPAA
FMADTPAYSI YCRLLGMKVG KDAHLGSVGF GAADLIEIGA DTSIGNEVFL NNVSIEGGML
HIGHIRIGTD CYVGSRAVVE RDAVMEDRAE LGNLSALSAD HTIPAGEIWN GSPASFTAKA
APETQPEHIT PLRRVVFDTA LSLVMAVFPV IAFVPLLPGM VIYDQLHDGR WSIGTVPLYA
LIPLLSVMYI SFMLAEIVIL RWLLLGRVKE GVYDVRSAFF LRKWFVDHLM ELALGAVHAI
YATLYVVPWM RALGAKIGEY TEISTATSVT HDLLDIGPEA FIADGVMLGD ADIRHGRLYL
RKTVIGRRSF VGNSALLPDG TSIPDECLVG CLSVPPATDK APLKDGQTCL GSPSFILPTR
QSFTCHAETL TFRPGPIRIG MRLLIEGIRV LLPPALFIAM LGHAMTCFDW TYDHYGLLAS
YAAVPFIYFA VMGIPSLLSV ALMKWVLIGR YQSAEVPMWT PFVWLSEAIT ATYEGLAVPF
LLDPFRGTPF LPWSWKLLGA KVGRRICADT TDLTEFDMVE IGDDAALDTN CGPQTHLFED
RVMKIGLVRL GARTSLGTMS IALYGSTVNE DARIGPLSLV MKGESIPAGT VWSGSPARRQ
S
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