ID A0A0X8XBP0_HALHR Unreviewed; 578 AA.
AC A0A0X8XBP0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
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 Synonyms=pbpB {ECO:0000313|EMBL:BAU58518.1};
GN ORFNames=HH1059_18290 {ECO:0000313|EMBL:BAU58518.1};
OS Halorhodospira halochloris (Ectothiorhodospira halochloris).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Halorhodospira.
OX NCBI_TaxID=1052 {ECO:0000313|EMBL:BAU58518.1, ECO:0000313|Proteomes:UP000218890};
RN [1] {ECO:0000313|Proteomes:UP000218890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM-1059 {ECO:0000313|Proteomes:UP000218890};
RA Tsukatani Y.;
RT "Halorhodospira halochloris DSM-1059 complete genome sequence.";
RL Submitted (FEB-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; AP017372; BAU58518.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0X8XBP0; -.
DR KEGG; hhk:HH1059_18290; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000218890; Chromosome.
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; 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:BAU58518.1};
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:UP000218890};
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 16..38
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
FT DOMAIN 62..210
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 251..546
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT ACT_SITE 298
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
SQ SEQUENCE 578 AA; 63118 MW; 386E98D663C6AA02 CRC64;
MARSKRQRKD AGGPPFWRLA VVMVATAGVV LALVGRALDL QVLNRDFLRD EAEARHLRTV
AISAYRGMIT DRNGAPLAVS SPVYSSWANP AEVLQEEGGV AELARALGRS EADLREYLER
RKQREFVYLR RHMPPDLSAQ IRSLDIPGVN LQRELRRFYP AGQTAAQLIG FTDIDGRGLE
GVERALDEPL SGEQGAKRVM RDRLGRVIDD VELIREPRPG EDVELSIDRD IQYLAFRELK
RAVHRHRAES GSVVVLDVHT GELLAVANKP SFNPHQRAQM DPEARRNRAF ANAYEPGSVI
KPFTIAAALR SGSVSPQESF DTAPGTMRVG RHTVRDLLDY GELDLAGVMQ KSSNVGAAKV
ALQTPPRELW QVMQDFEFGA PSGVSFASES AGHLDASPPR GEVRQATWSY GYGMSTTPVQ
LARSYAALAN GGVIRPVTIL RQEEEVEGHR VLDEDIAQQI RSMLETVIEP GGTGVRASVP
GYRVAGKTGT VRKAVAGGYS EDEYIAMFVG YAPAENPRIA VAVVIDDPAG EAYYGGQVAA
PVFSEVASGA LRILNVPPQA PPSGMPRIVA DWEEGRYD
//
