FTSI_HAEIN
ID FTSI_HAEIN Reviewed; 610 AA.
AC P45059;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 142.
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:0000255|HAMAP-Rule:MF_02080};
DE Short=PBP-3 {ECO:0000255|HAMAP-Rule:MF_02080};
GN Name=ftsI {ECO:0000255|HAMAP-Rule:MF_02080}; OrderedLocusNames=HI_1132;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
CC -!- FUNCTION: Catalyzes cross-linking of the peptidoglycan cell wall at the
CC division septum. {ECO:0000255|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: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}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_02080}.
CC -!- SIMILARITY: Belongs to the transpeptidase family. FtsI subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_02080}.
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DR EMBL; L42023; AAC22787.1; -; Genomic_DNA.
DR PIR; G64184; G64184.
DR RefSeq; NP_439290.1; NC_000907.1.
DR RefSeq; WP_005693446.1; NC_000907.1.
DR PDB; 6HZO; X-ray; 2.44 A; A/B/C/D=250-585.
DR PDBsum; 6HZO; -.
DR AlphaFoldDB; P45059; -.
DR SMR; P45059; -.
DR STRING; 71421.HI_1132; -.
DR DrugBank; DB00303; Ertapenem.
DR EnsemblBacteria; AAC22787; AAC22787; HI_1132.
DR KEGG; hin:HI_1132; -.
DR PATRIC; fig|71421.8.peg.1182; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_6_2_6; -.
DR OMA; HGKEEYY; -.
DR PhylomeDB; P45059; -.
DR BioCyc; HINF71421:G1GJ1-1165-MON; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000000579; 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; Hydrolase; Membrane;
KW Peptidoglycan synthesis; Protease; Reference proteome; Septation;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..610
FT /note="Peptidoglycan D,D-transpeptidase FtsI"
FT /id="PRO_0000195457"
FT TRANSMEM 43..65
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02080"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 327
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02080"
FT HELIX 258..275
FT /evidence="ECO:0007829|PDB:6HZO"
FT STRAND 278..286
FT /evidence="ECO:0007829|PDB:6HZO"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:6HZO"
FT STRAND 291..297
FT /evidence="ECO:0007829|PDB:6HZO"
FT HELIX 326..329
FT /evidence="ECO:0007829|PDB:6HZO"
FT HELIX 330..339
FT /evidence="ECO:0007829|PDB:6HZO"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:6HZO"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:6HZO"
FT STRAND 368..370
FT /evidence="ECO:0007829|PDB:6HZO"
FT HELIX 372..377
FT /evidence="ECO:0007829|PDB:6HZO"
FT HELIX 381..389
FT /evidence="ECO:0007829|PDB:6HZO"
FT HELIX 394..403
FT /evidence="ECO:0007829|PDB:6HZO"
FT HELIX 430..435
FT /evidence="ECO:0007829|PDB:6HZO"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:6HZO"
FT HELIX 446..457
FT /evidence="ECO:0007829|PDB:6HZO"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:6HZO"
FT HELIX 482..498
FT /evidence="ECO:0007829|PDB:6HZO"
FT HELIX 500..502
FT /evidence="ECO:0007829|PDB:6HZO"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:6HZO"
FT STRAND 510..520
FT /evidence="ECO:0007829|PDB:6HZO"
FT STRAND 523..536
FT /evidence="ECO:0007829|PDB:6HZO"
FT STRAND 543..551
FT /evidence="ECO:0007829|PDB:6HZO"
FT HELIX 564..575
FT /evidence="ECO:0007829|PDB:6HZO"
FT TURN 576..579
FT /evidence="ECO:0007829|PDB:6HZO"
SQ SEQUENCE 610 AA; 67166 MW; 8A1DA5538235C0A3 CRC64;
MVKFNSSRKS GKSKKTIRKL TAPETVKQNK PQKVFEKCFM RGRYMLSTVL ILLGLCALVA
RAAYVQSINA DTLSNEADKR SLRKDEVLSV RGSILDRNGQ LLSVSVPMSA IVADPKTMLK
ENSLADKERI AALAEELGMT ENDLVKKIEK NSKSGYLYLA RQVELSKANY IRRLKIKGII
LETEHRRFYP RVEEAAHVVG YTDIDGNGIE GIEKSFNSLL VGKDGSRTVR KDKRGNIVAH
ISDEKKYDAQ DVTLSIDEKL QSMVYREIKK AVSENNAESG TAVLVDVRTG EVLAMATAPS
YNPNNRVGVK SELMRNRAIT DTFEPGSTVK PFVVLTALQR GVVKRDEIID TTSFKLSGKE
IVDVAPRAQQ TLDEILMNSS NRGVSRLALR MPPSALMETY QNAGLSKPTD LGLIGEQVGI
LNANRKRWAD IERATVAYGY GITATPLQIA RAYATLGSFG VYRPLSITKV DPPVIGKRVF
SEKITKDIVG ILEKVAIKNK RAMVEGYRVG VKTGTARKIE NGHYVNKYVA FTAGIAPISD
PRYALVVLIN DPKAGEYYGG AVSAPVFSNI MGYALRANAI PQDAEAAENT TTKSAKRIVY
IGEHKNQKVN
