ID D3GMK4_9ENTR Unreviewed; 2035 AA.
AC D3GMK4;
DT 23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 23-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=High Molecular Weight Protein 2 (HMWP2) {ECO:0000313|EMBL:CAX65491.1};
GN Name=irp2 {ECO:0000313|EMBL:CAX65491.1};
OS Enterobacter hormaechei.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX NCBI_TaxID=158836 {ECO:0000313|EMBL:CAX65491.1};
RN [1] {ECO:0000313|EMBL:CAX65491.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=05-545 {ECO:0000313|EMBL:CAX65491.1};
RX PubMed=20084283; DOI=10.1371/journal.pone.0008662;
RA Paauw A., Leverstein-van Hall M.A., Verhoef J., Fluit A.C.;
RT "Evolution in quantum leaps: multiple combinatorial transfers of HPI and
RT other genetic modules in Enterobacteriaceae.";
RL PLoS ONE 5:e8662-e8662(2010).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; FN297818; CAX65491.1; -; Genomic_DNA.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0009403; P:toxin biosynthetic process; IEA:UniProt.
DR CDD; cd12114; A_NRPS_TlmIV_like; 1.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd19535; Cyc_NRPS; 2.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 3.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR PANTHER; PTHR45527:SF10; PHENYLOXAZOLINE SYNTHASE MBTB; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 3.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 3.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 3.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 15..91
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1404..1478
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1943..2017
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2035 AA; 228661 MW; 18B75F11D35756DC CRC64;
MISGAPSQDS LLPDNRHAAD YQQLRERLIQ ELNLTPQQLH EESNLIQAGL DSIRLMRWLH
WFRKNGYRLT LRELYAAPTL AAWNQLMLSR SPENAEEETP PDESSWPNMT ESTPFPLTPV
QHAYLTGRMP GQKLGGVGCH LYQEFEGHCL TASQLEQAIT TLLQRHPMLH IAFRPDGQQV
WLPQPYWNGV TVHDLRHNDA ESRQAYLDAL RQRLSHRLLR VEIGETFDFQ LTLLPDNRHR
LHVNIDLLIM DASSFTLFFD ELNALLAGES LPAIDTRYDF RSYLLHQQKI NQPLRDDARA
YWLAKASTLP PAPVLPLACE PATLREVRNT RRRMIVPATR WHAFSNRAGE YGVTPTMALA
TCFSAVLARW GGLTRLLLNI TLFDRQPLHP AVGAMLADFT NILLLDTACD GDTVSNLARK
NQLTFTEDWE HRHWSGVELL RELKRQQRYP HGAPVVFTSN LGRSLYSSRA ESPLGEPEWG
ISQTPQVWID HLAFEHHGEV WLQWDSNDAL FPTALVETLF DAYCQLINQL CDDESAWQKP
FADMMPASQR AIRERVNATG APIPEGLLHE GIFRIALQQP QALAVTDMRY QWNYHELTDY
ARRCAGRLIE CGVQPGDNVA ITMSKGAGQL VAVLAVLLAG AVYVPVSLDQ PAARREKIYA
DASVRLVLIC QHDASAGSDD IPVLAWQQAI EAEPIANPVV RAPTQPAYII YTSGSTGTPK
GVVISHRGAL NTCCDINTRY QVGPHDRVLA LSALHFDLSV YDIFGVLRAG GALVMVMENQ
RRDPHAWCEL IQRHQVTLWN SVPALFDMLL TWCEGFADAT PENLRAVMLS GDWIGLDLPA
RYRAFRPQGQ FIAMGGATEA SIWSNACEIH DVPAHWRSIP YGFPLTNQRY RVVDEQGRDC
PDWVPGELWI GGTGVAEGYF NDPLRSEQQF LTLPDERWYR TGDLGCYWPD GTIEFLGRRD
KQVKVGGYRI ELGEIESALS QLAGVKQATV LAIGEKEKTL AAYVVPQGEA FCITDHRNPA
LPQAWHTLAG TLPCCAISPE ISAEQVADFL QHRLLKLKPG HTAGADPLPL MNSLAIQPRW
QAVVERWLAF LVTQRRLKPA AEGYQVCAGE EREDEHPHFS GHDLTLSQIL RGARNELSLL
NDAQWSPESL AFNHPASAPY IQELATICQQ LAQRLQRPIR LLEVGTRTGR AAESLLAQLN
AGQIEYVGLE QSQEMLLSAR QRLAPWPGAR LSLWNADTLA AHAHSADIIW LNNALHRLLP
EDPGLLATLQ QLAVPGALLY VMEFRQLTPS ALLSTLLLTN GQPEALLHNS ADWAALFSAA
AFNCQHGDEV AGLQRFLVQC PDRQVRRDPR QLQAALAGRL PGWMVPQRIV FLDALPLTAN
GKIDYQALKR RHTPEAENPA EADLPQGDIE KQVAALWQQL LSTGNVTRET DFFQQGGDSL
LATRLTGQLH QAGYEAQLSD LFNHPRLADF AATLRKTDVP VEQPFVHSPE DRYQPFALTD
VQQAYLVGRQ PGFALGGVGS HFFVEFEIAD LDLTRLETVW NRLIARHDML RAIVRDGQQQ
VLEQTPPWVI PAHTLHTPEE ALRVREKLAH QVLNPEVWPV FDLQVGYVDG MPARLWLCLD
NLLLDGLSMQ ILLAELEHGY RYPQQLLPPL PVTFRDYLQQ PSLQSPNPDS LAWWQAQLDD
IPPAPALPLR CLPQEVETPR FARLNGALDS TRWHRLKKRA ADAHLTPSAV LLSVWSTVLS
AWSAQPEFTL NLTLFDRRPL HPQINQILGD FTSLMLLSWH PGESWLHSAQ SLQQRLSQNL
NHRDVSAIRV MRQLAQQQNV PAVPMPVVFT SALGFEQDNF LARRNLLKPV WGISQTPQVW
LDHQIYESEG ELRFNWDFVA ALFPAGQVER QFEQYCALLN RMAEDESGWQ LPLAALVPPV
KHAGQCAERS PRVCPEQSQP HIAADESTVS LICDAFREVV GESVTPAENF FEAGATSLNL
VQLHVLLQRH EFSTLTLLDL FTHPSPAALA DYLAGVATVE KTKRPRPVRR RQRRI
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