ID I4VVF4_9GAMM Unreviewed; 604 AA.
AC I4VVF4;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Peptidoglycan D,D-transpeptidase FtsI {ECO:0000256|HAMAP-Rule:MF_02080};
DE EC=3.4.16.4 {ECO:0000256|HAMAP-Rule:MF_02080};
DE AltName: Full=Penicillin-binding protein 3 {ECO:0000256|HAMAP-Rule:MF_02080};
DE Short=PBP-3 {ECO:0000256|HAMAP-Rule:MF_02080};
GN Name=ftsI {ECO:0000256|HAMAP-Rule:MF_02080};
GN ORFNames=UU7_14123 {ECO:0000313|EMBL:EIL91195.1};
OS Rhodanobacter spathiphylli B39.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1163407 {ECO:0000313|EMBL:EIL91195.1, ECO:0000313|Proteomes:UP000003226};
RN [1] {ECO:0000313|EMBL:EIL91195.1, ECO:0000313|Proteomes:UP000003226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B39 {ECO:0000313|EMBL:EIL91195.1,
RC ECO:0000313|Proteomes:UP000003226};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
CC -!- FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the
CC division septum. {ECO:0000256|HAMAP-Rule:MF_02080}.
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:0000256|HAMAP-
CC Rule:MF_02080};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02080}.
CC -!- SIMILARITY: Belongs to the transpeptidase family. FtsI subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_02080}.
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:EIL91195.1}.
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DR EMBL; AJXT01000045; EIL91195.1; -; Genomic_DNA.
DR RefSeq; WP_007809396.1; NZ_AJXT01000045.1.
DR AlphaFoldDB; I4VVF4; -.
DR STRING; 1163407.UU7_14123; -.
DR PATRIC; fig|1163407.3.peg.2843; -.
DR eggNOG; COG0768; Bacteria.
DR OrthoDB; 9766847at2; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000003226; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
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; IEA:UniProtKB-KW.
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; 3.30.450.330; -; 1.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 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 PANTHER; PTHR30627; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE; 1.
DR PANTHER; PTHR30627:SF1; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE FTSI; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645, ECO:0000256|HAMAP-
KW Rule:MF_02080}; Cell cycle {ECO:0000256|HAMAP-Rule:MF_02080};
KW Cell division {ECO:0000256|HAMAP-Rule:MF_02080,
KW ECO:0000313|EMBL:EIL91195.1};
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_02080};
KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_02080};
KW Cell shape {ECO:0000256|HAMAP-Rule:MF_02080};
KW Cell wall biogenesis/degradation {ECO:0000256|HAMAP-Rule:MF_02080};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_02080};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_02080};
KW Peptidoglycan synthesis {ECO:0000256|HAMAP-Rule:MF_02080};
KW Protease {ECO:0000256|HAMAP-Rule:MF_02080};
KW Reference proteome {ECO:0000313|Proteomes:UP000003226};
KW Septation {ECO:0000256|HAMAP-Rule:MF_02080};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_02080};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_02080}.
FT DOMAIN 69..217
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 258..555
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT REGION 579..604
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 305
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
SQ SEQUENCE 604 AA; 65083 MW; E2E6D3DC98B79FA5 CRC64;
MSWRKHVKPS PPGRRRVAGP SARRRMIVVV GLLGLVSAAL VARAFDLQVV RKEFYQRQGD
ARFLREVPIP VSRGTIFDRN GEPLAVSTPM MSIWANPSEV LDNDERIPAL AQALGVEADG
LKAQLAQRSD REFVYLRRQM SPAAAQAVLD LGIPGINGQR EFKRYYPSGE VTAHVLGFTN
IDDRGQEGLE LAYDEWLAGK PGAKRVIRDR MGHVVEDLEQ VRAPKPGQNL TLSIDRRIQF
LAYNELKNTL EKSQADSGSM VVLDVRTGEV LAMVNLPTYN PNALGGSKPG QRRNRAMTDV
LEPGSTIKPI LMAAALSSGK YTPTSPLIDT TGGHWYFQGH DIHDTHNYGV LTPTGVITKS
SNVGAAHIAM QLDTSLMYDT YRAFGFGNST ESGFPGEASG YLRIGRDWRP LEKAILGYGY
GLNVTVLQLA NAYATIADGG VMHSPTFIKD NDSTAKQIIS PEVAHELLQM METVTGPGST
GTMARIANYS VAGKTGTAHK AAGGSYAKSN YTSAFAGIVP ASSPRLAAVV VIDNPQKGSY
YGGTVSGPVF SKVMEGALRL LDVPPDNIGR WYVGGPLQSP DGLVGSKPPV DAPIDDAPVD
EDTP
//
