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Database: UniProt
Entry: U5C257_9BACT
LinkDB: U5C257_9BACT
Original site: U5C257_9BACT 
ID   U5C257_9BACT            Unreviewed;       796 AA.
AC   U5C257;
DT   11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT   11-DEC-2013, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=Penicillin amidase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=P872_05170 {ECO:0000313|EMBL:ERM83006.1};
OS   Rhodonellum psychrophilum GCM71 = DSM 17998.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC   Rhodonellum.
OX   NCBI_TaxID=1123057 {ECO:0000313|EMBL:ERM83006.1, ECO:0000313|Proteomes:UP000016843};
RN   [1] {ECO:0000313|EMBL:ERM83006.1, ECO:0000313|Proteomes:UP000016843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GCM71 {ECO:0000313|EMBL:ERM83006.1,
RC   ECO:0000313|Proteomes:UP000016843};
RX   PubMed=24309741;
RA   Hauptmann A.L., Glaring M.A., Hallin P.F., Prieme A., Stougaard P.;
RT   "Draft Genome Sequence of the Psychrophilic and Alkaliphilic Rhodonellum
RT   psychrophilum Strain GCM71T.";
RL   Genome Announc. 1:e01014-13(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:ERM83006.1}.
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DR   EMBL; AWXR01000019; ERM83006.1; -; Genomic_DNA.
DR   RefSeq; WP_019598779.1; NZ_KB906682.1.
DR   AlphaFoldDB; U5C257; -.
DR   MEROPS; S45.003; -.
DR   PATRIC; fig|1123057.7.peg.2140; -.
DR   eggNOG; COG2366; Bacteria.
DR   OrthoDB; 9759796at2; -.
DR   Proteomes; UP000016843; Unassembled WGS sequence.
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:SF5; PENICILLIN G ACYLASE; 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   Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016843};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   ACT_SITE        250
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         322
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         325
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   796 AA;  89923 MW;  350DC58E1136D2C0 CRC64;
     MKKLVLVLLF MLILGTVGYQ IAKFNFGPKY NGEITLEGLN AETEVFFDDF GVPHIYASSA
     EDAYQTLGYV HAQDRLFQME MMRRVGTGTL AELLGEDLLD VDKFFRTLGI PQHAQMSTAA
     WHSEGDSEWK SATEAYIKGV NQFILEGKIP IEYTLLGSKP RDFTINDVHA VVGYMSFTFA
     MAVKTDPLIT KMSRQLGPDY MKALSVHTLP EHHIIPNNYP KRDSVSLQIK TNTSLACLLE
     KLPVPLFMGS NAWVIAPSRT ASGEVIFCND THIGFSQPSV WYEAHLEYPG FSYYGNHLAG
     VPFGLVGHTR THSIGLTMFE NDDQDFFEEK LNPNNPNETI YGTGFSPIKS RMDTIKIKDK
     DHVLFEIRET NHGPILNAVV PEIAGMTDNP VASWWVYVLE PTRAIEATWK MGHAKNIQEV
     EDGARLIHAP GLNIMYGDKT GNIAWWASAK LPIRPAHVNS KIFLDGTNPL DEHTGWIPFE
     ENPMSINPES GFVATSNNQP DTLSNGMYYP GYYYPGDRWD RISKTIMSRN DWTQESIKTL
     QLESINETQP KNAKLLLSEI SKTDFPEDEA ILNALGDWSG EHGLEEIAPT LYYKWIYHIL
     SEMMVDELGE EDFQNYLGTF MAVRSTPLLL QSENSPWWDN KNTPKIENRK DIINKALSKS
     LTELHAQHGS NSRKWQWRKS ILSEHPHPLG AKKPLDRIFN VSTNPMAANE ESVNKLAFTL
     NGEGIYKVNS GPAMRIILDF ANVDASESIL PTGQSGNLFS PWYKDQAAMF VEGHYRPQLM
     KEEVIKGTYR KKLVFK
//
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