FTSI_PSEAE
ID FTSI_PSEAE Reviewed; 579 AA.
AC G3XD46;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 16-NOV-2011, sequence version 1.
DT 03-AUG-2022, entry version 68.
DE RecName: Full=Peptidoglycan D,D-transpeptidase FtsI {ECO:0000255|HAMAP-Rule:MF_02080};
DE EC=3.4.16.4 {ECO:0000255|HAMAP-Rule:MF_02080};
DE AltName: Full=Penicillin-binding protein 3 {ECO:0000303|PubMed:20580675};
DE Short=PBP-3 {ECO:0000303|PubMed:20580675};
GN Name=ftsI {ECO:0000303|PubMed:20580675}; Synonyms=pbpB;
GN OrderedLocusNames=PA4418 {ECO:0000312|EMBL:AAG07806.1};
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 29-39, SUBCELLULAR LOCATION, AND PENICILLIN-BINDING.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=20580675; DOI=10.1016/j.pep.2010.05.005;
RA de Leon S.R., Daniels K., Clarke A.J.;
RT "Production and purification of the penicillin-binding protein 3 from
RT Pseudomonas aeruginosa.";
RL Protein Expr. Purif. 73:177-183(2010).
RN [3]
RP INDUCTION.
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).
RN [4] {ECO:0007744|PDB:3PBN, ECO:0007744|PDB:3PBO, ECO:0007744|PDB:3PBQ, ECO:0007744|PDB:3PBR, ECO:0007744|PDB:3PBS, ECO:0007744|PDB:3PBT}
RP X-RAY CRYSTALLOGRAPHY (1.64 ANGSTROMS) OF 50-579 OF APOPROTEIN AND IN
RP COMPLEXES WITH CEFTAZIDIME; IMIPENEM; MEROPENEM; AZTREONAM AND MC-1.
RX PubMed=21135211; DOI=10.1073/pnas.1013092107;
RA Han S., Zaniewski R.P., Marr E.S., Lacey B.M., Tomaras A.P., Evdokimov A.,
RA Miller J.R., Shanmugasundaram V.;
RT "Structural basis for effectiveness of siderophore-conjugated monocarbams
RT against clinically relevant strains of Pseudomonas aeruginosa.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:22002-22007(2010).
RN [5] {ECO:0007744|PDB:4KQO, ECO:0007744|PDB:4KQQ, ECO:0007744|PDB:4KQR}
RP X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 35-579 IN COMPLEXES WITH
RP PIPERACILLIN AND (5S)-PENICILLOIC ACID.
RX PubMed=23899657; DOI=10.1021/cb400200h;
RA van Berkel S.S., Nettleship J.E., Leung I.K., Brem J., Choi H.,
RA Stuart D.I., Claridge T.D., McDonough M.A., Owens R.J., Ren J.,
RA Schofield C.J.;
RT "Binding of (5S)-penicilloic acid to penicillin binding protein 3.";
RL ACS Chem. Biol. 8:2112-2116(2013).
CC -!- FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the
CC division septum (By similarity). Binds penicillin (PubMed:20580675).
CC {ECO:0000255|HAMAP-Rule:MF_02080, ECO:0000269|PubMed:20580675}.
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:20580675}; Single-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_02080}.
CC -!- INDUCTION: Mainly produced during exponential phase of growth.
CC {ECO:0000269|PubMed:9045804}.
CC -!- SIMILARITY: Belongs to the transpeptidase family. FtsI subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02080}.
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DR EMBL; AE004091; AAG07806.1; -; Genomic_DNA.
DR PIR; S54872; S54872.
DR RefSeq; NP_253108.1; NC_002516.2.
DR RefSeq; WP_003094139.1; NZ_QZGE01000004.1.
DR PDB; 3PBN; X-ray; 2.00 A; A=50-579.
DR PDB; 3PBO; X-ray; 1.74 A; A=50-579.
DR PDB; 3PBQ; X-ray; 1.70 A; A=50-579.
DR PDB; 3PBR; X-ray; 1.95 A; A=50-579.
DR PDB; 3PBS; X-ray; 2.00 A; A=50-579.
DR PDB; 3PBT; X-ray; 1.64 A; A=50-579.
DR PDB; 4KQO; X-ray; 2.31 A; A/B=35-579.
DR PDB; 4KQQ; X-ray; 2.10 A; A/B=35-579.
DR PDB; 4KQR; X-ray; 2.01 A; A/B=35-579.
DR PDB; 6HR4; X-ray; 1.19 A; A=50-579.
DR PDB; 6HR6; X-ray; 2.53 A; A=47-579.
DR PDB; 6HR9; X-ray; 1.99 A; A=50-579.
DR PDB; 6HZR; X-ray; 1.19 A; A=50-579.
DR PDB; 6I1E; X-ray; 1.64 A; A=50-579.
DR PDB; 6R3X; X-ray; 1.59 A; A=50-563.
DR PDB; 6R40; X-ray; 2.20 A; A=50-579.
DR PDB; 6R42; X-ray; 1.72 A; A=50-579.
DR PDB; 6UN1; X-ray; 2.26 A; A=50-579.
DR PDB; 6UN3; X-ray; 1.90 A; A=50-579.
DR PDB; 6VJE; X-ray; 1.76 A; A=50-579.
DR PDB; 6VOT; X-ray; 2.40 A; A=50-579.
DR PDB; 6Y6U; X-ray; 1.55 A; A=50-563.
DR PDB; 6Y6Z; X-ray; 1.70 A; A=50-563.
DR PDB; 7ATM; X-ray; 1.58 A; A=50-579.
DR PDB; 7ATO; X-ray; 1.59 A; A=50-579.
DR PDB; 7ATW; X-ray; 1.44 A; A=50-579.
DR PDB; 7ATX; X-ray; 1.79 A; A=50-579.
DR PDB; 7AU0; X-ray; 2.17 A; A=50-579.
DR PDB; 7AU1; X-ray; 1.36 A; A=50-579.
DR PDB; 7AU8; X-ray; 1.79 A; A=50-579.
DR PDB; 7AU9; X-ray; 2.14 A; A=50-579.
DR PDB; 7AUB; X-ray; 1.91 A; A=50-579.
DR PDB; 7AUH; X-ray; 2.01 A; A=50-579.
DR PDB; 7JWL; X-ray; 2.20 A; A=50-579.
DR PDB; 7KIT; X-ray; 2.09 A; A=1-579.
DR PDB; 7KIV; X-ray; 2.39 A; A=1-579.
DR PDB; 7KIW; X-ray; 2.49 A; A=1-579.
DR PDB; 7LC4; X-ray; 2.00 A; A=50-579.
DR PDB; 7ONK; X-ray; 1.73 A; A/B=39-563.
DR PDB; 7ONX; X-ray; 2.16 A; A=39-563.
DR PDB; 7ONY; X-ray; 1.77 A; A=39-563.
DR PDB; 7ONZ; X-ray; 1.86 A; A=39-563.
DR PDBsum; 3PBN; -.
DR PDBsum; 3PBO; -.
DR PDBsum; 3PBQ; -.
DR PDBsum; 3PBR; -.
DR PDBsum; 3PBS; -.
DR PDBsum; 3PBT; -.
DR PDBsum; 4KQO; -.
DR PDBsum; 4KQQ; -.
DR PDBsum; 4KQR; -.
DR PDBsum; 6HR4; -.
DR PDBsum; 6HR6; -.
DR PDBsum; 6HR9; -.
DR PDBsum; 6HZR; -.
DR PDBsum; 6I1E; -.
DR PDBsum; 6R3X; -.
DR PDBsum; 6R40; -.
DR PDBsum; 6R42; -.
DR PDBsum; 6UN1; -.
DR PDBsum; 6UN3; -.
DR PDBsum; 6VJE; -.
DR PDBsum; 6VOT; -.
DR PDBsum; 6Y6U; -.
DR PDBsum; 6Y6Z; -.
DR PDBsum; 7ATM; -.
DR PDBsum; 7ATO; -.
DR PDBsum; 7ATW; -.
DR PDBsum; 7ATX; -.
DR PDBsum; 7AU0; -.
DR PDBsum; 7AU1; -.
DR PDBsum; 7AU8; -.
DR PDBsum; 7AU9; -.
DR PDBsum; 7AUB; -.
DR PDBsum; 7AUH; -.
DR PDBsum; 7JWL; -.
DR PDBsum; 7KIT; -.
DR PDBsum; 7KIV; -.
DR PDBsum; 7KIW; -.
DR PDBsum; 7LC4; -.
DR PDBsum; 7ONK; -.
DR PDBsum; 7ONX; -.
DR PDBsum; 7ONY; -.
DR PDBsum; 7ONZ; -.
DR AlphaFoldDB; G3XD46; -.
DR SMR; G3XD46; -.
DR STRING; 287.DR97_1596; -.
DR DrugCentral; G3XD46; -.
DR PaxDb; G3XD46; -.
DR PRIDE; G3XD46; -.
DR EnsemblBacteria; AAG07806; AAG07806; PA4418.
DR GeneID; 881247; -.
DR KEGG; pae:PA4418; -.
DR PATRIC; fig|208964.12.peg.4627; -.
DR PseudoCAP; PA4418; -.
DR HOGENOM; CLU_009289_6_2_6; -.
DR InParanoid; G3XD46; -.
DR OMA; HGKEEYY; -.
DR PhylomeDB; G3XD46; -.
DR BRENDA; 2.4.1.129; 5087.
DR UniPathway; UPA00219; -.
DR EvolutionaryTrace; G3XD46; -.
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 3D-structure; Carboxypeptidase; Cell cycle; Cell division;
KW Cell inner membrane; Cell membrane; Cell shape;
KW Cell wall biogenesis/degradation; Direct protein sequencing; Hydrolase;
KW Membrane; Peptidoglycan synthesis; Protease; Reference proteome; Septation;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..579
FT /note="Peptidoglycan D,D-transpeptidase FtsI"
FT /id="PRO_0000438878"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02080"
FT REGION 558..579
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 294
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02080"
FT STRAND 50..58
FT /evidence="ECO:0007829|PDB:6HR4"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:7ONZ"
FT STRAND 72..84
FT /evidence="ECO:0007829|PDB:6HR4"
FT HELIX 86..89
FT /evidence="ECO:0007829|PDB:6HR4"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:6HR4"
FT HELIX 96..103
FT /evidence="ECO:0007829|PDB:6HR4"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:6HR4"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:6HR4"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:6HR4"
FT HELIX 131..138
FT /evidence="ECO:0007829|PDB:6HR4"
FT STRAND 145..154
FT /evidence="ECO:0007829|PDB:6HR4"
FT HELIX 158..161
FT /evidence="ECO:0007829|PDB:6HR4"
FT HELIX 162..165
FT /evidence="ECO:0007829|PDB:6HR4"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:7ATM"
FT HELIX 177..181
FT /evidence="ECO:0007829|PDB:6HR4"
FT HELIX 183..187
FT /evidence="ECO:0007829|PDB:6HR4"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:6HR4"
FT STRAND 203..211
FT /evidence="ECO:0007829|PDB:6HR4"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:6HR4"
FT HELIX 225..241
FT /evidence="ECO:0007829|PDB:6HR4"
FT STRAND 245..253
FT /evidence="ECO:0007829|PDB:6HR4"
FT TURN 254..256
FT /evidence="ECO:0007829|PDB:6HR4"
FT STRAND 258..266
FT /evidence="ECO:0007829|PDB:6HR4"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:6R42"
FT HELIX 278..281
FT /evidence="ECO:0007829|PDB:6HR4"
FT HELIX 284..287
FT /evidence="ECO:0007829|PDB:6HR4"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:7AU1"
FT HELIX 293..296
FT /evidence="ECO:0007829|PDB:6HR4"
FT HELIX 297..306
FT /evidence="ECO:0007829|PDB:6HR4"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:7AU1"
FT STRAND 315..317
FT /evidence="ECO:0007829|PDB:6HR4"
FT STRAND 321..325
FT /evidence="ECO:0007829|PDB:6HR4"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:6HR4"
FT STRAND 338..341
FT /evidence="ECO:0007829|PDB:6HR4"
FT HELIX 342..347
FT /evidence="ECO:0007829|PDB:6HR4"
FT HELIX 351..361
FT /evidence="ECO:0007829|PDB:6HR4"
FT HELIX 363..373
FT /evidence="ECO:0007829|PDB:6HR4"
FT TURN 374..376
FT /evidence="ECO:0007829|PDB:6HR4"
FT HELIX 399..406
FT /evidence="ECO:0007829|PDB:6HR4"
FT TURN 407..410
FT /evidence="ECO:0007829|PDB:3PBO"
FT STRAND 412..414
FT /evidence="ECO:0007829|PDB:7ONZ"
FT HELIX 415..426
FT /evidence="ECO:0007829|PDB:6HR4"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:6HR4"
FT STRAND 435..437
FT /evidence="ECO:0007829|PDB:6HR4"
FT STRAND 446..449
FT /evidence="ECO:0007829|PDB:7KIW"
FT HELIX 451..466
FT /evidence="ECO:0007829|PDB:6HR4"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:6HR9"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:6HR4"
FT STRAND 482..488
FT /evidence="ECO:0007829|PDB:6HR4"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:6I1E"
FT STRAND 504..512
FT /evidence="ECO:0007829|PDB:6HR4"
FT STRAND 513..515
FT /evidence="ECO:0007829|PDB:6Y6U"
FT STRAND 518..526
FT /evidence="ECO:0007829|PDB:6HR4"
FT STRAND 527..529
FT /evidence="ECO:0007829|PDB:7ONX"
FT TURN 534..537
FT /evidence="ECO:0007829|PDB:7AU1"
FT HELIX 539..552
FT /evidence="ECO:0007829|PDB:6HR4"
FT HELIX 560..562
FT /evidence="ECO:0007829|PDB:4KQR"
FT TURN 565..569
FT /evidence="ECO:0007829|PDB:4KQR"
SQ SEQUENCE 579 AA; 62856 MW; 983D0F43C66A7218 CRC64;
MKLNYFQGAL YPWRFCVIVG LLLAMVGAIV WRIVDLHVID HDFLKGQGDA RSVRHIAIPA
HRGLITDRNG EPLAVSTPVT TLWANPKELM TAKERWPQLA AALGQDTKLF ADRIEQNAER
EFIYLVRGLT PEQGEGVIAL KVPGVYSIEE FRRFYPAGEV VAHAVGFTDV DDRGREGIEL
AFDEWLAGVP GKRQVLKDRR GRVIKDVQVT KNAKPGKTLA LSIDLRLQYL AHRELRNALL
ENGAKAGSLV IMDVKTGEIL AMTNQPTYNP NNRRNLQPAA MRNRAMIDVF EPGSTVKPFS
MSAALASGRW KPSDIVDVYP GTLQIGRYTI RDVSRNSRQL DLTGILIKSS NVGISKIAFD
IGAESIYSVM QQVGLGQDTG LGFPGERVGN LPNHRKWPKA ETATLAYGYG LSVTAIQLAH
AYAALANDGK SVPLSMTRVD RVPDGVQVIS PEVASTVQGM LQQVVEAQGG VFRAQVPGYH
AAGKSGTARK VSVGTKGYRE NAYRSLFAGF APATDPRIAM VVVIDEPSKA GYFGGLVSAP
VFSKVMAGAL RLMNVPPDNL PTATEQQQVN AAPAKGGRG
