ID R7XSI1_9ACTN Unreviewed; 873 AA.
AC R7XSI1;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Penicillin amidase {ECO:0000313|EMBL:EON22302.1};
GN ORFNames=CF8_3846 {ECO:0000313|EMBL:EON22302.1};
OS Nocardioides sp. CF8.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=110319 {ECO:0000313|EMBL:EON22302.1, ECO:0000313|Proteomes:UP000015971};
RN [1] {ECO:0000313|EMBL:EON22302.1, ECO:0000313|Proteomes:UP000015971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF8 {ECO:0000313|EMBL:EON22302.1,
RC ECO:0000313|Proteomes:UP000015971};
RX PubMed=23833136;
RA Kimbrel J.A., Chang J., Arp D.J., Sayavedra-Soto L.A.;
RT "The Draft Genome Sequence of Nocardioides sp. Strain CF8 Reveals the Scope
RT of Its Metabolic Capabilities.";
RL Genome Announc. 1:e00439-e00439(2013).
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:EON22302.1}.
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DR EMBL; ASEP01000107; EON22302.1; -; Genomic_DNA.
DR AlphaFoldDB; R7XSI1; -.
DR STRING; 110319.CF8_3846; -.
DR MEROPS; S45.003; -.
DR PATRIC; fig|110319.3.peg.418; -.
DR eggNOG; COG2366; Bacteria.
DR HOGENOM; CLU_011790_0_1_11; -.
DR OrthoDB; 5240333at2; -.
DR Proteomes; UP000015971; Chromosome.
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:UP000015971};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT TRANSMEM 28..51
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 306
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 218
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 387
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 873 AA; 95604 MW; 40C63A476462C57A CRC64;
MTEQPATTPD DDFSLRTLFR KAPRGLRWSA YVAAALALLL VVLLVTAVAF VRRPVPETDG
ALELAGLEGH VEVIRDDHGI PQIYADTDAD LMRAQGFVAA QDRFFEMDVR RHVTAGRLSE
LFGEDGLETD KYIRTMGWRR VAEQEWALLE TETRDALTAY AQGVNAYLDQ LGTSEIAVEY
TILGLTGLDY EPEPWEPADS LAWLKAMAWD LRGNMDDEIA RVMASLDHTE EEIAELYPAY
DPEAHPPIVG TGGVVDEVFE QNASGNSTRN PRRPAFDAEA VRTLVDLKAG LDRMPELLGR
GEGIGSNSWV VDGEHSATGQ PLLANDPHLG ISQPGIWMQT GLHCREITPD CTLDVAGFTF
SGVPGVIIGH NADIAWGFTN LGPDVTDLYL EQVEGATWIQ DGKPRPLTLR TETIKVRDGD
DFVLHIRETA HGPLLSDVSR ELSTVGANAP TDQPGERGNG YAVALQWTAL RPTTTADAVL
GLNRAGDWDE FRAAASDFAV PAQNMVYADR DGHIGYQAPG LVPIRKSGNT GAMPAEGWLS
ANDWTGDFIP FDGLPNVLDP EEGFIVTANQ AVIDDDYPYF LTDDWDAGYR STRIRELLAE
EGELSVGEMT RLQLDTANPM APTLVPYLLD IEDLGSPYYR DGQELLADWD FTQPADSAAA
AYYNAVWSNL LRLTFHDELR EGIWPDGGDR WFAVVTDLLT DPAGPWWDDS ETEDVTESRD
DILSQAMRDA RDELTMRQSL DADDWTWGHL HQLDLHHSTL GESGVAPIER LFNRDGRGVG
GGPSIVDATS WNAALGYGVT AAPSMRMVVS LADFDASRYI NLTGVSGHPG SSHYGDQTEL
FVNGDYLPWA FTRDAVVEAG EDTLVLTPAG AAD
//
