ID B6IV20_RHOCS Unreviewed; 811 AA.
AC B6IV20;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE SubName: Full=Penicillin acylase II, putative {ECO:0000313|EMBL:ACJ00144.1};
DE EC=3.5.1.11 {ECO:0000313|EMBL:ACJ00144.1};
GN Name=acyII {ECO:0000313|EMBL:ACJ00144.1};
GN OrderedLocusNames=RC1_2771 {ECO:0000313|EMBL:ACJ00144.1};
OS Rhodospirillum centenum (strain ATCC 51521 / SW).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospirillum.
OX NCBI_TaxID=414684 {ECO:0000313|EMBL:ACJ00144.1, ECO:0000313|Proteomes:UP000001591};
RN [1] {ECO:0000313|Proteomes:UP000001591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RA Touchman J.W., Bauer C., Blankenship R.E.;
RT "Genome sequence of Rhodospirillum centenum.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACJ00144.1, ECO:0000313|Proteomes:UP000001591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51521 / SW {ECO:0000313|Proteomes:UP000001591};
RX PubMed=20500872; DOI=10.1186/1471-2164-11-325;
RA Lu Y.K., Marden J., Han M., Swingley W.D., Mastrian S.D., Chowdhury S.R.,
RA Hao J., Helmy T., Kim S., Kurdoglu A.A., Matthies H.J., Rollo D.,
RA Stothard P., Blankenship R.E., Bauer C.E., Touchman J.W.;
RT "Metabolic flexibility revealed in the genome of the cyst-forming alpha-1
RT proteobacterium Rhodospirillum centenum.";
RL BMC Genomics 11:325-325(2010).
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}.
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DR EMBL; CP000613; ACJ00144.1; -; Genomic_DNA.
DR AlphaFoldDB; B6IV20; -.
DR STRING; 414684.RC1_2771; -.
DR MEROPS; S45.003; -.
DR KEGG; rce:RC1_2771; -.
DR eggNOG; COG2366; Bacteria.
DR HOGENOM; CLU_011790_4_0_5; -.
DR Proteomes; UP000001591; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008953; F:penicillin amidase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:ACJ00144.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000001591};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT TRANSMEM 21..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 276
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 354
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 357
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 811 AA; 85824 MW; 2885B57F910BE1FC CRC64;
MPVGSSRRAR RSPGRRVARG AGIAALGLLG LGAVAAGAAW IYLGASRPLL EGSLALPGLS
APVTVARDAG GVPTVTGTSR ADVAHALGFL HGQERFFQMD TIRRSAAGEL AALVGDAALP
LDRKRRVHRF RARMQAELAA LPADDRAVLD AYTAGVNQGL AALGATPFEY ALLGGEPQPW
APEDSLLAVV AMYFDLQDEE GGLDRRLAQA RATLGPALAD FLYPVGTSWD APIDGTRLDA
PPLPGPEALP PGFPRRTAGL EGAAAPVAED ATVPGSNNWA VAGSHSSHGG AIVANDMHLG
HGVPNLWYRA RLVVTGTGEA PVLDATGVTL PGAPNIVAGS NGRVAWGYTN SQIDTGDVVV
LEPGAAGGDS YRTPEGDRTP VVAEERICSV SGPCETLTVR ETVWGPVIAE EGGLRLAYRW
VAHDTGARAL GAALELERAG DVEEAVRIAH RSAIPNQNLM LADRDGRIAW TIIGRVPARV
GFDGRTPVSF ADGSRRWDGF LPPDRVPAVI DPQAGRLWSA NSRVVGGEAF ALLGDGGYAH
GSRARQIRDA LLAQERFDEK ALLAIQLDDR GTVLDRWHGL MLEAVKARAD DPAVADMLAY
LTDWDNRAVP EAVGYRLVRT FRAELLTALY GAFVAPPETE GPAAFRLASR QADEPAWRLL
TERPAHLVPP GFAGWDAVVA AALDKVREDV AKAAGGDLSR YRWGERNRAA IRHPLSRFVP
GLGWLTDAPA DRLPGDVYQP RAQSPSFGAS ERFAVSPGRE AQGLFQMPGG QSGHPLAPYY
LAGHDDWVAG RPVPFLPGPA RWTLRLEPGA S
//
