ID A0A0G3UJM9_9ACTN Unreviewed; 521 AA.
AC A0A0G3UJM9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Surfactin hydrolase {ECO:0000313|EMBL:AKL65115.1};
GN Name=sfhA {ECO:0000313|EMBL:AKL65115.1};
GN ORFNames=M444_06610 {ECO:0000313|EMBL:AKL65115.1};
OS Streptomyces sp. Mg1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=465541 {ECO:0000313|EMBL:AKL65115.1, ECO:0000313|Proteomes:UP000035653};
RN [1] {ECO:0000313|EMBL:AKL65115.1, ECO:0000313|Proteomes:UP000035653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mg1 {ECO:0000313|EMBL:AKL65115.1,
RC ECO:0000313|Proteomes:UP000035653};
RX PubMed=23908282;
RA Hoefler B.C., Konganti K., Straight P.D.;
RT "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using PacBio
RT Single-Molecule Sequencing.";
RL Genome Announc. 1:e00535-13(2013).
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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DR EMBL; CP011664; AKL65115.1; -; Genomic_DNA.
DR RefSeq; WP_037795014.1; NZ_DS570452.1.
DR AlphaFoldDB; A0A0G3UJM9; -.
DR ESTHER; 9actn-a0a0g3ujm9; Tiancimycin-TnmK-Tripeptidase-HIP.
DR KEGG; strm:M444_06610; -.
DR PATRIC; fig|465541.12.peg.1516; -.
DR OrthoDB; 4447445at2; -.
DR Proteomes; UP000035653; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR013595; Pept_S33_TAP-like_C.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AKL65115.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000035653};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..521
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002561007"
FT DOMAIN 91..242
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 394..493
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
FT REGION 489..521
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 521 AA; 56211 MW; B16971EA77D2BA0C CRC64;
MRMKRFAPLL AAAGLVATTV PLLSATQATA APGPDYGARK PAWHRCGADT PASYECATIK
VPLDYSRPQG RKLDLAISRI KSENPAKRHG VLLLNPGGPG GTGLDLPLMT AEAMPKEVRD
QFDLVGFDPR GVGQSSPISC GLTDAEQNMD RPYRKATFGA DVEWARTVAD KCRAKAGAVL
PHITTRNTAR DLDAIRAALG ERKISYLGYS YGTYLGAVYT QMFPNRTDRF VLDSGVDPQR
IWRGMIQVWA TEAEPAFKRW TEWTAERSGE FGLGDSPKAV SQTFWALVAR ADKDPIVVDD
MKITGDDIRA SRGVFFYPAQ AAPFVKSLKD AADGKAPSAA AAATELKRTL RPAEPATDNG
TAVFWSVVCG DTGAWPRDPE QYRRDAVKDK AAYPLYGDFA SNIKPCAFWQ RPVEAATPMK
TRANVMTVQN EWDSQTPLTS GQGLHRALGG SKMVLVKGGE GHGVYLADPN SCANAPVSAY
LTTGKLPAKD VTCQTPPAAA ERRASQAPQK PLPLPSTPGR F
//
