ID D9XR93_9ACTN Unreviewed; 370 AA.
AC D9XR93;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Secreted pectinesterase {ECO:0000313|EMBL:EFL42040.1};
GN ORFNames=SSRG_04844 {ECO:0000313|EMBL:EFL42040.1};
OS Streptomyces griseoflavus Tu4000.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=467200 {ECO:0000313|EMBL:EFL42040.1, ECO:0000313|Proteomes:UP000002968};
RN [1] {ECO:0000313|EMBL:EFL42040.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tu4000 {ECO:0000313|EMBL:EFL42040.1};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces griseoflavus strain Tu4000.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the pectinesterase family.
CC {ECO:0000256|ARBA:ARBA00008891}.
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DR EMBL; GG657758; EFL42040.1; -; Genomic_DNA.
DR RefSeq; WP_004932905.1; NZ_GG657758.1.
DR AlphaFoldDB; D9XR93; -.
DR STRING; 467200.SSRG_04844; -.
DR eggNOG; COG4677; Bacteria.
DR HOGENOM; CLU_012243_3_1_11; -.
DR OrthoDB; 112037at2; -.
DR Proteomes; UP000002968; Unassembled WGS sequence.
DR GO; GO:0045330; F:aspartyl esterase activity; IEA:UniProtKB-KW.
DR GO; GO:0030599; F:pectinesterase activity; IEA:InterPro.
DR GO; GO:0042545; P:cell wall modification; IEA:InterPro.
DR Gene3D; 2.160.20.10; Single-stranded right-handed beta-helix, Pectin lyase-like; 1.
DR InterPro; IPR012334; Pectin_lyas_fold.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR InterPro; IPR000070; Pectinesterase_cat.
DR InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR31321; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR PANTHER; PTHR31321:SF141; ACYL-COA THIOESTER HYDROLASE YBHC-RELATED; 1.
DR Pfam; PF01095; Pectinesterase; 1.
DR SUPFAM; SSF51126; Pectin lyase-like; 1.
DR PROSITE; PS51318; TAT; 1.
PE 3: Inferred from homology;
KW Aspartyl esterase {ECO:0000256|ARBA:ARBA00023085};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023085};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..370
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039097346"
FT DOMAIN 55..341
FT /note="Pectinesterase catalytic"
FT /evidence="ECO:0000259|Pfam:PF01095"
FT REGION 351..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 370 AA; 39781 MW; EBF8D8DF2BC0CE08 CRC64;
MPSPLSRRNF LLTGATAGTA LALTAFPARA SHRPRGPFGR YGSPSDRLTP GTLYVHPGGA
GDFTGVQDAV TAATGAGRTL VIAPGTYRGT VSVDADRTGM TWIGASEDPR DVVIVHDNAA
GTPKPDGSGT YGTSGSATAT VRPDGFTARW ITFANDWLRT DLPGTSGTQA VALKVQGDRS
AFTHCRFLGH QDTLYADSPS VDTFARQYFS HCYAEGDVDF VFGRATAVFE RCHFRTLVRP
DLTAAPYGFV FAPSTAGANP HGYLVTRSRI SSEAPDGYYK LARPWVPSSD RTARPMLTVR
ETHLGAGIDA VAPYTDMSSG YPWQDQRFAE YRNTGPGAVV TVPENRPRLT PAEAASHTRE
AYLGDWRPRR
//
