ID A0A1B8UJF0_9BACL Unreviewed; 803 AA.
AC A0A1B8UJF0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Beta-lactam antibiotic acylase {ECO:0000313|EMBL:OBY76455.1};
GN ORFNames=BBG47_27025 {ECO:0000313|EMBL:OBY76455.1};
OS Paenibacillus sp. KS1.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1849249 {ECO:0000313|EMBL:OBY76455.1, ECO:0000313|Proteomes:UP000092663};
RN [1] {ECO:0000313|EMBL:OBY76455.1, ECO:0000313|Proteomes:UP000092663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KS1 {ECO:0000313|EMBL:OBY76455.1,
RC ECO:0000313|Proteomes:UP000092663};
RA Lata P., Govindarajan S., Qi F., Li J.-L., Sahoo M.K.;
RT "Deep sequencing identified Paenibacillus in Kanamycin resistant culture
RT isolate from epiphyte Tillandsia usneoides (Spanish moss) in central
RT Florida, USA.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR001227-2};
CC Note=Binds 1 Ca(2+) ion per dimer. {ECO:0000256|PIRSR:PIRSR001227-2};
CC -!- SIMILARITY: Belongs to the peptidase S45 family.
CC {ECO:0000256|ARBA:ARBA00006586}.
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:OBY76455.1}.
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DR EMBL; MAIS01000160; OBY76455.1; -; Genomic_DNA.
DR RefSeq; WP_065294323.1; NZ_MAIS01000160.1.
DR AlphaFoldDB; A0A1B8UJF0; -.
DR OrthoDB; 9759796at2; -.
DR Proteomes; UP000092663; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR CDD; cd03747; Ntn_PGA_like; 1.
DR Gene3D; 1.10.1400.10; -; 1.
DR Gene3D; 2.30.120.10; -; 1.
DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR Gene3D; 1.10.439.10; Penicillin Amidohydrolase, domain 1; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR014395; Pen/GL7ACA/AHL_acylase.
DR InterPro; IPR043147; Penicillin_amidase_A-knob.
DR InterPro; IPR023343; Penicillin_amidase_dom1.
DR InterPro; IPR043146; Penicillin_amidase_N_B-knob.
DR InterPro; IPR002692; S45.
DR PANTHER; PTHR34218:SF4; ACYL-HOMOSERINE LACTONE ACYLASE QUIP; 1.
DR PANTHER; PTHR34218; PEPTIDASE S45 PENICILLIN AMIDASE; 1.
DR Pfam; PF01804; Penicil_amidase; 1.
DR PIRSF; PIRSF001227; Pen_acylase; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR001227-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000092663};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT TRANSMEM 23..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 265
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 337
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 340
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 803 AA; 90052 MW; 54801884647E3590 CRC64;
MKLLAAVTVP SVRRHKKKRW PRITGIIVLV FVLLLACAGG YVYWFVNKSL PVVQGKLNIS
GLEKEVTVWR DASGVPHIEA QNEHDLYMAQ GYVTAQDRMF QMDMSRRQAS GQLSEVVGAK
AIDRDKFFRA FSLRRAAEVS LGAYSKESRQ VLQWYADGVN NYIKHAKAAS SLPVEFAILG
YEPGEWQPVD SLTIGKYMSY DLAGNWEGQA FRYAMAQKLS TEKFQSLMPT YPKDGAMIIQ
ALKDQPIDLT ALAATAVPRD PFNGSNNWVV SGEKSASGKP MLANDPHLGL STPSIWYETH
LSAPELKVSG VIFAGVPGII LGHNDTIAWG VTNLSPDVQD LYIEKRNPDN PHQFEYMGNW
EDAKVYQEEI KVKGEAPVPY EVVVTRHGPI ISEFAHDQRQ ETALAMKWTA LDATTELEAV
QMFAKAQNWE DFKQALTHFE APAQNFVFAS TDGTIAYRGN GLIPIRKKGD GSVPVPGWTD
EYEWTGYIPW DELPTTVNPK EGFIATANNK VIGDSYPYHL TDVWSQPYRE ARIQQVLSAK
DKLTVEDMKK LQFDRHNLQA EEFVDELIAK IKDSPDLRQI DRDVLSLLQG WNKVNDPDQA
APLGFELWMQ GFDNVLFKSE INADLMELFN NKSVVKDEML RRALQGEREP WIDEKGGIEK
VALQAFQLAV DQAVSLQGKH PDKWQWGKFH QVDFAHPLGA VKPLDLIFNA KSVPMGGGRV
TVGAAGWDAE SGEVTHGAPW RTVIDMSDPT HSWNVVGPGQ SGHVLSKWYH DQVDDWTTGQ
YHITSIEPNE YRKAGNELKL VPE
//
