FTSI_CAUVN
ID FTSI_CAUVN Reviewed; 589 AA.
AC B8H0A0;
DT 28-NOV-2012, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Probable peptidoglycan D,D-transpeptidase FtsI {ECO:0000305};
DE EC=3.4.16.4 {ECO:0000250|UniProtKB:P0AD68};
DE AltName: Full=Penicillin-binding protein 3;
DE Short=PBP-3;
GN Name=ftsI; OrderedLocusNames=CCNA_02643;
OS Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=565050;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NA1000 / CB15N;
RX PubMed=20472802; DOI=10.1128/jb.00255-10;
RA Marks M.E., Castro-Rojas C.M., Teiling C., Du L., Kapatral V.,
RA Walunas T.L., Crosson S.;
RT "The genetic basis of laboratory adaptation in Caulobacter crescentus.";
RL J. Bacteriol. 192:3678-3688(2010).
RN [2]
RP SUBCELLULAR LOCATION, AND DOMAIN.
RC STRAIN=NA1000 / CB15N;
RX PubMed=18786147; DOI=10.1111/j.1365-2958.2008.06432.x;
RA Costa T., Priyadarshini R., Jacobs-Wagner C.;
RT "Localization of PBP3 in Caulobacter crescentus is highly dynamic and
RT largely relies on its functional transpeptidase domain.";
RL Mol. Microbiol. 70:634-651(2008).
RN [3]
RP INTERACTION WITH FTSN AND FTSW.
RC STRAIN=NA1000 / CB15N;
RX PubMed=21685367; DOI=10.1101/gad.2038911;
RA Modell J.W., Hopkins A.C., Laub M.T.;
RT "A DNA damage checkpoint in Caulobacter crescentus inhibits cell division
RT through a direct interaction with FtsW.";
RL Genes Dev. 25:1328-1343(2011).
CC -!- FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the
CC division septum. {ECO:0000250|UniProtKB:P0AD68}.
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;
CC Evidence={ECO:0000250|UniProtKB:P0AD68};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000250|UniProtKB:P0AD68}.
CC -!- SUBUNIT: Interacts with FtsN and FtsW. {ECO:0000269|PubMed:21685367}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:18786147}; Single-pass membrane protein
CC {ECO:0000269|PubMed:18786147}. Note=Localization varies during the cell
CC cycle. At the beginning of the cell cycle, it accumulates at the new
CC cell pole. Later during the cell cycle, polar accumulation disappears
CC concomitantly with the re-localization to the FtsZ ring in a FtsZ-
CC dependent manner. A portion of FtsI molecules is also diffusely
CC dispersed around the membrane during both cell elongation and division.
CC -!- DOMAIN: The active site is important for FtsI localization.
CC {ECO:0000269|PubMed:18786147}.
CC -!- SIMILARITY: Belongs to the transpeptidase family. {ECO:0000305}.
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; CP001340; ACL96108.1; -; Genomic_DNA.
DR RefSeq; WP_010920416.1; NC_011916.1.
DR RefSeq; YP_002518016.1; NC_011916.1.
DR AlphaFoldDB; B8H0A0; -.
DR SMR; B8H0A0; -.
DR PRIDE; B8H0A0; -.
DR EnsemblBacteria; ACL96108; ACL96108; CCNA_02643.
DR GeneID; 7332745; -.
DR KEGG; ccs:CCNA_02643; -.
DR PATRIC; fig|565050.3.peg.2591; -.
DR HOGENOM; CLU_009289_6_2_5; -.
DR OMA; EHYDPSM; -.
DR OrthoDB; 213680at2; -.
DR PhylomeDB; B8H0A0; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001364; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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 InterPro; IPR012338; Beta-lactam/transpept-like.
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.
DR PROSITE; PS00146; BETA_LACTAMASE_A; 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; Hydrolase;
KW Membrane; Peptidoglycan synthesis; Protease; Reference proteome; Septation;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..589
FT /note="Probable peptidoglycan D,D-transpeptidase FtsI"
FT /id="PRO_0000420269"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 296
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0AD68"
SQ SEQUENCE 589 AA; 62995 MW; 9C6F6817850BC1DE CRC64;
MSLSNLGPGG VHSPLWRWVV ERVWRLEHAF ERSRAAARPE DDTRIRIFLV MGFFGFCFVG
VSLGAGWSAL FSRAGQGGGY AQGVEGARGD VVDRNGKLLA VDLAHYALYV DPREVWDAKE
TRAALGRALP QVPAKRLDKA VFGDHRAFVL GGLTPDEKDA IFNLGLPGVT FEEQERRMYP
LGPTAAHLIG FVDSGGKGLA GAERALDDPI RKAAGGEGGP AQLSIDVRVQ AALEDELRKA
AEEFTPKGAV GLVTNVHTGE ILGMASWPDY DANKAGGATD DQRLNRAAAS VYEMGSTFKA
FTVAIGLDTG VATAASTFDA REPYKLGYRT IHDYHATKAV LNLVEVFQHS SNIGTAMLAE
RVGGQRLSQY FTNLGLTKPA KVELQESARP LTPRKWDQDT VASTSFGHGM NISPLALAQA
MNALLNGGEM RPLTIRKLPP GVRPEGRRVL SEHTSAEMLK IMRANVVPGE GGSGGKADVP
GLSVGGKTGT GEKYDPAIRR YNHQRQVSSF AATFPTDGPL EADRYFVLIL LDEPKGNANS
FGFSTGGWVA APAAGRVIER IAPFLGVKRK TELVTIANSP KNAAPEAGL
