ID A0A0Q7YU23_9SPHN Unreviewed; 525 AA.
AC A0A0Q7YU23;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Serine hydrolase {ECO:0000313|EMBL:KQZ64900.1};
GN ORFNames=ASD67_10835 {ECO:0000313|EMBL:KQZ64900.1};
OS Sphingopyxis sp. Root1497.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1736474 {ECO:0000313|EMBL:KQZ64900.1, ECO:0000313|Proteomes:UP000051141};
RN [1] {ECO:0000313|Proteomes:UP000051141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1497 {ECO:0000313|Proteomes:UP000051141};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQZ64900.1, ECO:0000313|Proteomes:UP000051141}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1497 {ECO:0000313|EMBL:KQZ64900.1,
RC ECO:0000313|Proteomes:UP000051141};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KQZ64900.1}.
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DR EMBL; LMGF01000003; KQZ64900.1; -; Genomic_DNA.
DR RefSeq; WP_056346719.1; NZ_LMGF01000003.1.
DR AlphaFoldDB; A0A0Q7YU23; -.
DR STRING; 1736474.ASD67_10835; -.
DR OrthoDB; 5377981at2; -.
DR Proteomes; UP000051141; Unassembled WGS sequence.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 2.40.128.600; -; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR001466; Beta-lactam-related.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR021860; Peptidase_S12_Pab87-rel_C.
DR PANTHER; PTHR46825; D-ALANYL-D-ALANINE-CARBOXYPEPTIDASE/ENDOPEPTIDASE AMPH; 1.
DR PANTHER; PTHR46825:SF9; PROTEIN FLP; 1.
DR Pfam; PF00144; Beta-lactamase; 1.
DR Pfam; PF11954; DUF3471; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:KQZ64900.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..525
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5006331176"
FT DOMAIN 30..369
FT /note="Beta-lactamase-related"
FT /evidence="ECO:0000259|Pfam:PF00144"
FT DOMAIN 417..519
FT /note="Peptidase S12 Pab87-related C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11954"
SQ SEQUENCE 525 AA; 58120 MW; A33C8750119074EF CRC64;
MKHVRLLAFA LLATAAMPAW AEPPKDIAES VEALRKEIGA TGVSIAIVED GKTTLSRGWG
ERKLGERGQV DGQTIFQTGS TGKAMTAAAL AILVDEGKIA WDDPVIKHMP WFRMYDAWVT
REITIRDLLV HRSGLGLGQG DLMFVPRTNL TRKQTVERVA YLKPQTSFRS SYAYDNILYA
VAGQLIEEVS GQTWEAFMRD RVLRPGGMKN ATSDSEDRFR IANRSWPHAR LNGPLRGLGD
QQALDERDEL GRNGAPAGGL AMSADDMAAW LKIQLAHGAL PNGKALFSAA QAAEMWKPVT
PMPITELPAA LKPAQPMQQA YALGWQVQDY RGHRIVQHSG GVFGSITRVV MIPDKNVGFA
IMMNSEESGM LLGLTFKLID HYLDQPDYGW TTKWQDWYKE RLAGGVEYLK QTQATPAKVG
PSLDPARYAG RYRDPWYGDI VVANTAKGLT IDFTSTPRMI GRLKHWQYDS FVTEYDDPAI
EPAYVTFALD ADGKVTGVTM KAVSKIADFS WDYHDLALKP VEGAK
//
