ID S5TA31_9GAMM Unreviewed; 579 AA.
AC S5TA31;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=CYCME_2289 {ECO:0000313|EMBL:AGS40601.1};
OS Cycloclasticus zancles 78-ME.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Cycloclasticus.
OX NCBI_TaxID=1198232 {ECO:0000313|EMBL:AGS40601.1, ECO:0000313|Proteomes:UP000015380};
RN [1] {ECO:0000313|EMBL:AGS40601.1, ECO:0000313|Proteomes:UP000015380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7-ME {ECO:0000313|Proteomes:UP000015380};
RA Yakimov M.M., Messina E., Genovese M., Denaro R., Crisafi F., Russo D.,
RA Cappello S., Santisi S., Smedile F., Golyshina O.V., Tran H., Pieper D.H.,
RA Golyshin P.N., Giuliano L.;
RT "Between feast and famine: a lifestyle of most important marine PAH-
RT degrading bacterium Cycloclasticus sp. 7ME.";
RL Submitted (MAY-2013) 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; CP005996; AGS40601.1; -; Genomic_DNA.
DR RefSeq; WP_015005171.1; NC_021917.1.
DR AlphaFoldDB; S5TA31; -.
DR KEGG; cza:CYCME_2289; -.
DR PATRIC; fig|1198232.3.peg.2259; -.
DR eggNOG; COG0768; Bacteria.
DR HOGENOM; CLU_009289_6_2_6; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000015380; 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; 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:AGS40601.1};
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 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 26..43
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
FT DOMAIN 67..213
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 255..551
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT ACT_SITE 302
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02080"
SQ SEQUENCE 579 AA; 63120 MW; 5A01AD59AE35CAE8 CRC64;
MKYSHQQSNN TVQKVIVPEL AGRRRFILAC FMLMMCVLIY RAIDLQVLNN SYLQKRGEAV
HLRDIKLPAY RGKITDVGGH ALAISAPVSS VWVNPQELEL GTKKKEFAKL LGLKVSALDK
KLKKVASRRF VYLRRHMDPQ VTAMIDQLQL PGVYLQKEYR RYYPDGEVAA HLVGFTNIDD
EGQEGLELAW DESLKGSAGA ERVLRDGKRR MVKHVDNIRA PIPGQDIRLT IDRRLQYLAY
RELKAAVAQQ KATSGSLVLL NAETGQLLAV ANQPAFNPND RSKIKASHVR NRAFVDLFEP
GSTMKPFTVA AGMESGVFDA STVIDTNPGY MRVGRSQVRD HRNYGEIDLA TLLLKSSNVA
SAKIALGIPG EKLWGMLNSL GFGQSAGLGF PGEARGKLVG YEQWRPIETA TLSFGYGLST
SALQLARAYS VIANEGVLEP ISLVVDEAAA ESVRVMSPTV ANSVRNMMRG VVTKAGTAPR
AKVYGYSVAG KTGTVKKAIA GGYAEDKYLG VFAGMAPASD PKLVMVVVID EPKAGDYYGG
LVAAPVFSRV MSGALRLMNI APDNLDKATV FASLERGIQ
//