FTSI2_PSEAE
ID FTSI2_PSEAE Reviewed; 565 AA.
AC Q9I1K1;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Probable peptidoglycan D,D-transpeptidase PbpC {ECO:0000305};
DE EC=3.4.16.4 {ECO:0000255|HAMAP-Rule:MF_02080};
DE AltName: Full=PBP3x {ECO:0000303|PubMed:9045804};
DE AltName: Full=Penicillin-binding protein 3 homolog {ECO:0000303|PubMed:9045804};
DE Short=PBP3 homolog {ECO:0000303|PubMed:9045804};
GN Name=pbpC {ECO:0000303|PubMed:9045804};
GN OrderedLocusNames=PA2272 {ECO:0000312|EMBL:AAG05660.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP PROTEIN SEQUENCE OF 2-7, PENICILLIN-BINDING, SUBCELLULAR LOCATION,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9045804; DOI=10.1128/jb.179.5.1490-1496.1997;
RA Liao X., Hancock R.E.W.;
RT "Identification of a penicillin-binding protein 3 homolog, PBP3x, in
RT Pseudomonas aeruginosa: gene cloning and growth phase-dependent
RT expression.";
RL J. Bacteriol. 179:1490-1496(1997).
CC -!- FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the
CC division septum (By similarity). Binds penicillin (PubMed:9045804).
CC {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:9045804}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also
CC transpeptidation of peptidyl-alanyl moieties that are N-acyl
CC substituents of D-alanine.; EC=3.4.16.4; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02080};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_02080}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02080, ECO:0000269|PubMed:9045804}; Single-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_02080}.
CC -!- INDUCTION: Produced in the stationary phase of growth.
CC {ECO:0000269|PubMed:9045804}.
CC -!- DISRUPTION PHENOTYPE: Inactivation causes no changes in the cell
CC morphology or growth rate of exponentially growing cells.
CC {ECO:0000269|PubMed:9045804}.
CC -!- SIMILARITY: Belongs to the transpeptidase family. FtsI subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02080}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE004091; AAG05660.1; -; Genomic_DNA.
DR PIR; A83361; A83361.
DR RefSeq; NP_250962.1; NC_002516.2.
DR RefSeq; WP_003113747.1; NZ_QZGE01000014.1.
DR AlphaFoldDB; Q9I1K1; -.
DR SMR; Q9I1K1; -.
DR STRING; 287.DR97_6161; -.
DR PaxDb; Q9I1K1; -.
DR PRIDE; Q9I1K1; -.
DR DNASU; 882173; -.
DR EnsemblBacteria; AAG05660; AAG05660; PA2272.
DR GeneID; 882173; -.
DR KEGG; pae:PA2272; -.
DR PATRIC; fig|208964.12.peg.2374; -.
DR PseudoCAP; PA2272; -.
DR HOGENOM; CLU_009289_6_2_6; -.
DR InParanoid; Q9I1K1; -.
DR OMA; IVMESKT; -.
DR PhylomeDB; Q9I1K1; -.
DR BioCyc; PAER208964:G1FZ6-2311-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0008658; F:penicillin binding; IBA:GO_Central.
DR GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-UniRule.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; -; 1.
DR HAMAP; MF_02080; FtsI_transpept; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR037532; FtsI_transpept.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56519; SSF56519; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
PE 1: Evidence at protein level;
KW Carboxypeptidase; Cell cycle; Cell division; Cell inner membrane;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW Direct protein sequencing; Hydrolase; Membrane; Peptidoglycan synthesis;
KW Protease; Reference proteome; Septation; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9045804"
FT CHAIN 2..565
FT /note="Probable peptidoglycan D,D-transpeptidase PbpC"
FT /id="PRO_0000438879"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02080"
FT ACT_SITE 289
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02080"
SQ SEQUENCE 565 AA; 61101 MW; 14C52121EAFC1FB0 CRC64;
MSSQRRNYRF ILVVTLFVLA SLAVSGRLVY LQVHDHEFLA DQGDLRSIRD LPIPVTRGMI
TDRNGEPLAV STEVASIWCN PREMAAHLDE VPRLAGALHR PAAALLAQLQ ANPNKRFLYL
ERGLSPIEAS EVMALGITGV HQIKEYKRFY PSSELTAQLI GLVNIDGRGQ EGTELGFNDW
LSGKDGVREV AINPRGSLVN SIKVLKTPKA SQDVALSIDL RLQFIAYKAL EKAVLKFGAH
SGSAVLVNPK SGQILAMANF PSYNPNNRAS FAPAFMRNRT LTDTFEPGSV IKPFSMSAAL
ASGKFDENSQ VSVAPGWMTI DGHTIHDVAR RDVLTMTGVL INSSNIGMSK VALQIGPKPI
LEQLGRVGFG APLSLGFPGE NPGYLPFHEK WSNIATASMS FGYSLAVNTA ELAQAYSVFA
NDGKLVPLSL LRDNPQNQVR QAMDPQIARR IRAMLQTVVE DPKGVVRARV PGYHVAGKSG
TARKASGRGY ADKSYRSLFV GMAPASDPQL VLAVMIDSPT RIGYFGGLVS APTFSDIMAG
SLRALAIPPD NLQDSPAVAD RQHHG
