ID   AGAR_STRCO              Reviewed;         309 AA.
AC   P07883;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 2.
DT   25-MAY-2022, entry version 132.
DE   RecName: Full=Extracellular agarase;
DE            EC=3.2.1.81;
DE   Flags: Precursor;
GN   Name=dagA; OrderedLocusNames=SCO3471; ORFNames=SCE65.07c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 31-61.
RC   STRAIN=A3(2) / NRRL B-16638;
RX   PubMed=17165236; DOI=10.1007/bf00329843;
RA   Buttner M.J., Fearnley I.M., Bibb M.J.;
RT   "The agarase gene (dagA) of Streptomyces coelicolor A3(2): nucleotide
RT   sequence and transcriptional analysis.";
RL   Mol. Gen. Genet. 209:101-109(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-D-galactosidic linkages in agarose,
CC         giving the tetramer as the predominant product.; EC=3.2.1.81;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Predicted to be exported by the Tat system. The position of the
CC       signal peptide cleavage has been experimentally proven.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
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DR   EMBL; X05811; CAA29257.1; -; Genomic_DNA.
DR   EMBL; AL939116; CAB61795.1; -; Genomic_DNA.
DR   PIR; S07322; EUSMAG.
DR   RefSeq; NP_627674.1; NC_003888.3.
DR   RefSeq; WP_011029010.1; NZ_VNID01000041.1.
DR   AlphaFoldDB; P07883; -.
DR   SMR; P07883; -.
DR   STRING; 100226.SCO3471; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   PRIDE; P07883; -.
DR   GeneID; 1098908; -.
DR   KEGG; sco:SCO3471; -.
DR   PATRIC; fig|100226.15.peg.3531; -.
DR   eggNOG; COG2273; Bacteria.
DR   HOGENOM; CLU_037753_0_0_11; -.
DR   InParanoid; P07883; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0033916; F:beta-agarase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd02178; GH16_beta_agarase; 1.
DR   InterPro; IPR016287; Beta_agarase.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   InterPro; IPR008263; GH16_AS.
DR   InterPro; IPR006311; TAT_signal.
DR   InterPro; IPR019546; TAT_signal_bac_arc.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   Pfam; PF10518; TAT_signal; 1.
DR   PIRSF; PIRSF001097; Agarase; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS01034; GH16_1; 1.
DR   PROSITE; PS51762; GH16_2; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Glycosidase; Hydrolase; Reference proteome;
KW   Secreted; Signal.
FT   SIGNAL          1..30
FT                   /note="Tat-type signal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00648,
FT                   ECO:0000269|PubMed:17165236"
FT   CHAIN           31..309
FT                   /note="Extracellular agarase"
FT                   /id="PRO_0000011797"
FT   DOMAIN          33..309
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   ACT_SITE        155
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT   ACT_SITE        160
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
SQ   SEQUENCE   309 AA;  35164 MW;  18E479E642DB1A43 CRC64;
     MVNRRDLIKW SAVALGAGAG LAGPAPAAHA ADLEWEQYPV PAAPGGNRSW QLLPSHSDDF
     NYTGKPQTFR GRWLDQHKDG WSGPANSLYS ARHSWVADGN LIVEGRRAPD GRVYCGYVTS
     RTPVEYPLYT EVLMRVSGLK LSSNFWLLSR DDVNEIDVIE CYGNESLHGK HMNTAYHIFQ
     RNPFTELARS QKGYFADGSY GYNGETGQVF GDGAGQPLLR NGFHRYGVHW ISATEFDFYF
     NGRLVRRLNR SNDLRDPRSR FFDQPMHLIL NTESHQWRVD RGIEPTDAEL ADPSINNIYY
     RWVRTYQAV