ESTA_STRSC
ID ESTA_STRSC Reviewed; 345 AA.
AC P22266;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Esterase;
DE EC=3.1.1.-;
DE Flags: Precursor;
GN Name=estA;
OS Streptomyces scabiei.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1930;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 40-69.
RC STRAIN=FL1;
RX PubMed=2254271; DOI=10.1128/jb.172.12.7020-7026.1990;
RA Raymer G., Willard J.M.A., Schottel J.L.;
RT "Cloning, sequencing, and regulation of expression of an extracellular
RT esterase gene from the plant pathogen Streptomyces scabies.";
RL J. Bacteriol. 172:7020-7026(1990).
RN [2]
RP SUBCELLULAR LOCATION.
RX PubMed=1612447; DOI=10.1016/0378-1119(92)90536-x;
RA Schottel J.L., Hale V., Babcock M.J.;
RT "Regulation and secretion of an extracellular esterase from Streptomyces
RT scabies.";
RL Gene 115:27-31(1992).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
RX PubMed=7773790; DOI=10.1038/nsb0395-218;
RA Wei Y., Schottel J.L., Derewenda U., Swenson L., Patkar S., Derewenda Z.S.;
RT "A novel variant of the catalytic triad in the Streptomyces scabies
RT esterase.";
RL Nat. Struct. Biol. 2:218-223(1995).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1612447}.
CC -!- INDUCTION: By zinc.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-5 is the initiator.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA26744.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M57297; AAA26743.1; -; Genomic_DNA.
DR EMBL; M57297; AAA26744.1; ALT_INIT; Genomic_DNA.
DR PIR; A37845; A37845.
DR PDB; 1ESC; X-ray; 2.10 A; A=40-345.
DR PDB; 1ESD; X-ray; 2.30 A; A=40-345.
DR PDB; 1ESE; X-ray; 2.40 A; A=40-345.
DR PDBsum; 1ESC; -.
DR PDBsum; 1ESD; -.
DR PDBsum; 1ESE; -.
DR AlphaFoldDB; P22266; -.
DR SMR; P22266; -.
DR DrugBank; DB02845; Methylphosphinic Acid.
DR EvolutionaryTrace; P22266; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR CDD; cd01823; SEST_like; 1.
DR Gene3D; 3.40.50.1110; -; 1.
DR InterPro; IPR037460; SEST-like.
DR InterPro; IPR013830; SGNH_hydro.
DR InterPro; IPR036514; SGNH_hydro_sf.
DR PANTHER; PTHR37981; PTHR37981; 1.
DR Pfam; PF13472; Lipase_GDSL_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Hydrolase;
KW Secreted; Serine esterase; Signal.
FT SIGNAL 1..39
FT /evidence="ECO:0000269|PubMed:2254271"
FT CHAIN 40..345
FT /note="Esterase"
FT /id="PRO_0000021208"
FT DISULFID 73..103
FT DISULFID 156..180
FT DISULFID 236..294
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:1ESC"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:1ESC"
FT TURN 57..59
FT /evidence="ECO:0007829|PDB:1ESC"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:1ESC"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:1ESC"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:1ESC"
FT HELIX 80..89
FT /evidence="ECO:0007829|PDB:1ESC"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:1ESC"
FT STRAND 94..100
FT /evidence="ECO:0007829|PDB:1ESC"
FT HELIX 108..111
FT /evidence="ECO:0007829|PDB:1ESC"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1ESD"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1ESC"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1ESD"
FT HELIX 127..130
FT /evidence="ECO:0007829|PDB:1ESC"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:1ESC"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:1ESC"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:1ESC"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:1ESC"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:1ESE"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:1ESC"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:1ESC"
FT TURN 184..186
FT /evidence="ECO:0007829|PDB:1ESC"
FT HELIX 188..214
FT /evidence="ECO:0007829|PDB:1ESC"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:1ESC"
FT HELIX 233..237
FT /evidence="ECO:0007829|PDB:1ESC"
FT TURN 247..250
FT /evidence="ECO:0007829|PDB:1ESC"
FT TURN 253..255
FT /evidence="ECO:0007829|PDB:1ESC"
FT HELIX 256..275
FT /evidence="ECO:0007829|PDB:1ESC"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:1ESC"
FT STRAND 280..282
FT /evidence="ECO:0007829|PDB:1ESC"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:1ESC"
FT STRAND 304..314
FT /evidence="ECO:0007829|PDB:1ESC"
FT STRAND 316..318
FT /evidence="ECO:0007829|PDB:1ESC"
FT HELIX 325..342
FT /evidence="ECO:0007829|PDB:1ESC"
SQ SEQUENCE 345 AA; 36670 MW; 237DC28EE185B00E CRC64;
MSSAMRKTTN SPVVRRLTAA AVALGSCLAL AGPAGSAGAA PADPVPTVFF GDSYTANFGI
APVTNQDSER GWCFQAKENY PAVATRSLAD KGITLDVQAD VSCGGALIHH FWEKQELPFG
AGELPPQQDA LKQDTQLTVG SLGGNTLGFN RILKQCSDEL RKPSLLPGDP VDGDEPAAKC
GEFFGTGDGK QWLDDQFERV GAELEELLDR IGYFAPDAKR VLVGYPRLVP EDTTKCLTAA
PGQTQLPFAD IPQDALPVLD QIQKRLNDAM KKAAADGGAD FVDLYAGTGA NTACDGADRG
IGGLLEDSQL ELLGTKIPWY AHPNDKGRDI QAKQVADKIE EILNR
