HMWP2_YERE8
ID HMWP2_YERE8 Reviewed; 2035 AA.
AC P48633; A1JTF8;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=High-molecular-weight protein 2;
DE Short=HMWP2;
GN Name=irp2; OrderedLocusNames=YE2617;
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8366034; DOI=10.1128/jb.175.17.5488-5504.1993;
RA Guilvout I., Mercereau-Puijalon O., Bonnefoy S., Pugsley A.P., Carniel E.;
RT "High-molecular-weight protein 2 of Yersinia enterocolitica is homologous
RT to AngR of Vibrio anguillarum and belongs to a family of proteins involved
RT in nonribosomal peptide synthesis.";
RL J. Bacteriol. 175:5488-5504(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081;
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(2006).
CC -!- FUNCTION: Unknown. May be involved in the nonribosomal synthesis of
CC small peptides.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000305};
CC Note=Binds 3 phosphopantetheines covalently. {ECO:0000305};
CC -!- DOMAIN: Consists of a central region with similarity to the repeat
CC domains of ACVS and GRC2, flanked by two repeat domains, each of which
CC contains 5 direct repeats.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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; L18881; AAA27636.1; -; Genomic_DNA.
DR EMBL; Z35454; CAA84606.1; -; Genomic_DNA.
DR EMBL; AM286415; CAL12654.1; -; Genomic_DNA.
DR PIR; A48654; A48654.
DR RefSeq; WP_011816641.1; NC_008800.1.
DR RefSeq; YP_001006815.1; NC_008800.1.
DR AlphaFoldDB; P48633; -.
DR SMR; P48633; -.
DR STRING; 393305.YE2617; -.
DR PRIDE; P48633; -.
DR EnsemblBacteria; CAL12654; CAL12654; YE2617.
DR KEGG; yen:YE2617; -.
DR PATRIC; fig|393305.7.peg.2780; -.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG2226; Bacteria.
DR eggNOG; COG3433; Bacteria.
DR HOGENOM; CLU_000022_40_0_6; -.
DR OMA; LYQEFDG; -.
DR Proteomes; UP000000642; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 3.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.30.559.10; -; 2.
DR Gene3D; 3.40.50.12780; -; 1.
DR Gene3D; 3.40.50.150; -; 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.
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 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; SSF47336; SSF47336; 3.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 3.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Ligase; Multifunctional enzyme; Phosphopantetheine; Phosphoprotein; Repeat.
FT CHAIN 1..2035
FT /note="High-molecular-weight protein 2"
FT /id="PRO_0000193096"
FT DOMAIN 15..91
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REPEAT 114..146
FT /note="I-DR1"
FT REPEAT 310..321
FT /note="I-DR2"
FT REPEAT 378..390
FT /note="I-DR3"
FT REPEAT 454..462
FT /note="I-DR4"
FT REPEAT 477..491
FT /note="I-DR5"
FT DOMAIN 1404..1478
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REPEAT 1495..1527
FT /note="II-DR1"
FT REPEAT 1682..1693
FT /note="II-DR2"
FT REPEAT 1750..1762
FT /note="II-DR3"
FT REPEAT 1826..1834
FT /note="II-DR4"
FT REPEAT 1849..1863
FT /note="II-DR5"
FT DOMAIN 1943..2017
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 3..547
FT /note="I"
FT REGION 1466..1919
FT /note="II"
FT MOD_RES 52
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1439
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1977
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2035 AA; 228827 MW; 1C801377A4375BDC CRC64;
MISGAPSKDS LLPDNRHAAD YQQLRERLIQ ELNLTPQQLH DESNLIQAGL DSIRLMRWLH
WFRKNGYRLT LRELYAAPTL AAWNQLMLSR SPENAEEETL PDESSWPNMT ESTPFPLTPV
QHAYLTGRMP GQTLGGVGCH LYQEFEGHCL TASQLEQAIT TLLQRHPMLH IAFRPDGQQV
WLPQPYWNGV TVHDLRHNDA ESRQAYLDAL RQRLSHRLLR VEIGETFDFQ LTLLPDNRHR
LHVNIDLLIM DASSFTLFFD ELNALLAGES LSAIDTRYDF RSYLLHQQKI NQPLRDDARA
YWLAKASTLP PAPVLPLVCE PATLREVRNT RRRMIVPATR WHAFSNRAGE YGVTPTMALA
TCFSAVLARW GGLTRLLLNI TLFDRQPLHP AVGAMLADFT NILLLDTACD GDTVSNLARK
NQLTFTEDWE HRHWSGVELL RELKRQQRYP HGAPVVFTSN LGRSLYSSRA ESPLGEPEWG
ISQTPQVWID HLAFEHHGEV WLQWDSNDAL FPPALVETLF DAYCQLINQL CDDESAWQKP
FADMMPASQR AIRERVNATG APIPEGLLHE GIFRIALQQP QALAVTDMRY QWNYHELTDY
ARRCAGRLVE CGVQPGDNVA ITMSKGAGQL VAVLAVLLAG AVYVPVSLDQ PAARREKIYA
DASVRLVLIC QHDASAGSDD IPVLAWQQAI EAEPIVNPVV RAPTQPAYII YTSGSTGTPK
GVVISHRGAL NTCCDINTRY QVGPHDRVLA LSALHFDLSV YDIFGVLRAG GALVMVMENQ
RRDPHAWCEL IQRHQVTLWN SVPALFDMLL TWCEGFADAT PENLRAVMLS GDWIGLDLPA
RYRAFRPQGQ FIAMGGATEA SIWSNACEIH DVPAHWRSIP YGFPLTNQRY RVVDERGRDC
PDWVSGELWI GGIGVAEGYF NDSLRSEQQF LTLPDERWYR TGDLGCYWPD GTIEFLGRRD
KQVKVGGYRI ELGEIESALS QLAGVKQATV LAIGEKEKTL AAYVVPQSEA FCVTDHRNPA
LPKAWHTLAG TLPCCAISPE ISAEQVADFL QHRLLKLKPG HTAGADPIPL MNSLAIQPRW
QAVVERWLAF LVTQRRLKPA AEGYQVCAGE EREDEHPHFS GHDLTLSQIL RGARNELSLL
NDAQWSPESL AFNHPASAPY IQELATICQQ LAQRLQRPVR LLEVGTRTGR AAESLLAQLN
AGQIEYVGLE QSQEMLLSAR QRLASWPGAR LSPWNADTLA AHAHSGDIIW LNNALHRLLP
EDPGLLATLQ QLAVPGALLY VMEFRQLTPS ALLSTLLLTN GQPEALLHNS ADWAALFSAA
AFNCQHSDEV AGLQRFLVQC PDRQVRRDPR QLQAALAGRL PGWMVPQRIV FLDALPLTAN
GKIDYQALKR RHTPKAENQA EADLPQGDIE KQVAALWQQL LSTGNVTRET DFFQQGGDSL
LATRLTGQLH QAGYEAQLSD LFNHPRLADF AATLRKIDVP VEQPFVHSPE ERYQPFALTD
VQQAYLVGRQ PGFTLGGVGS HFFVEFEIAD LDLTRLETVW NRLIARHDML RAVVLDGQQQ
VLEQTPPWVI PTHTLHTPEE ALRVREKLAH QVLNPEVWPV FDLQVGYVDG MPARLWLCLD
NLLLDGLSMQ ILLAELEHGY RYPQQLLPPL PVTFRDYLQQ PSLQSPNPDS LAWWQAQLDD
IPPAPALPLR CLPQEVETPR FARLNGALDS TRWHRLKKRA ADAHLTPSAV LLSVWSTVLS
AWSAQPEFTL NLTLFDRRPL HPQINQILGD FTSLMLLSWH PGESWLHSAQ SLQQRLSQNL
NHRDVSAIRV MRQLAQRQNV PAVPMPVVFT SALGFEQDNF LARRNLLKPV WGISQTPQVW
LDHQVYESEG ELRFNWDFVA ALFPAGQVER QFEQYCALLN RMAEDESSWQ LPLAALVPPV
KHAGQCAERP PRVCPEHSQP HIAADESTVS LICDAFREVV GESVTPAENF FEAGATSLNL
VQLHVLLQRH EFSTLTLLDL FTHPSPVALA DYLAGVATVE KTKRPRPVRR RQRRI