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Database: UniProt
Entry: A0A1H9ZCU4_9GAMM
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ID   A0A1H9ZCU4_9GAMM        Unreviewed;       593 AA.
AC   A0A1H9ZCU4;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=SAMN02583745_00521 {ECO:0000313|EMBL:SES79163.1};
OS   Thorsellia anophelis DSM 18579.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Thorselliaceae; Thorsellia.
OX   NCBI_TaxID=1123402 {ECO:0000313|EMBL:SES79163.1, ECO:0000313|Proteomes:UP000242642};
RN   [1] {ECO:0000313|Proteomes:UP000242642}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18579 {ECO:0000313|Proteomes:UP000242642};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_02080}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_02080}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family. FtsI subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_02080}.
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DR   EMBL; FOHV01000003; SES79163.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9ZCU4; -.
DR   STRING; 1123402.SAMN02583745_00521; -.
DR   OrthoDB; 9789078at2; -.
DR   UniPathway; UPA00219; -.
DR   Proteomes; UP000242642; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 1.10.150.770; -; 1.
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:SES79163.1};
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:UP000242642};
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   TRANSMEM        21..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
FT   DOMAIN          66..220
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          260..552
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   ACT_SITE        306
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
SQ   SEQUENCE   593 AA;  64910 MW;  DB04E4ECA1A4C82F CRC64;
     MNVAYHKKNL RKETPKANQS WRFMIVYTVL GAVFICLASY IAMIQIISPE YSIAQANKRS
     LRVQEIPPTR GMITDREGRP FAVSIPVKAV WIDPKFVLEQ GGVEHNDKWQ ALADTLGITV
     QEILAKVADN PSSRFTYLAR QVSIEKANYI QQLKLKGIGF KEESKRYYPT GPLVAQIVGI
     TNRDEKGIEG IELSFENWLQ GVPGERTIRK DKSGRVVETL DTIDSLSGQN LTLSIDERLQ
     NIVFREISKA VEVNKAVAAT AVLLDVHTGE VLAMASAPTY NPNMRQSVDD DLKRNRAITD
     VFEPGSTVKP LVVMAGLERG VIQPNTVLNT MPFVVNGKQI KDVSRQAQLS ITGVLQKSSN
     TGVSRIALAL QPDDLVDIYK KFGFAQPTRL GLVGEQSGYY PTKNRWSDIE RASFSYGYGL
     MITPMQLAKA YATIGSYGIS RPLSITRVDP PVSGEQVFNP DTVRTVLHMM ETVTHPGGGG
     VKAAVKDYRV AVKTGTAKKV ENGVYVDKYI AYTAGVAPVS NPRYSLVVVI NEPSAGEYFG
     GAVSAPVFSS IMGGVLRTMN IPPDGIEMSI EDPKIVVNTP QPVTLKNSRA VGG
//
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