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Database: UniProt
Entry: A0A1B6BCG8_9FIRM
LinkDB: A0A1B6BCG8_9FIRM
Original site: A0A1B6BCG8_9FIRM 
ID   A0A1B6BCG8_9FIRM        Unreviewed;       949 AA.
AC   A0A1B6BCG8;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Cell division protein peptidoglycan synthetase FtsI {ECO:0000313|EMBL:GAU77420.1};
DE            EC=2.4.1.129 {ECO:0000313|EMBL:GAU77420.1};
GN   ORFNames=F3D3_2049 {ECO:0000313|EMBL:GAU77420.1};
OS   Fusibacter sp. 3D3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XII. Incertae Sedis; Fusibacter.
OX   NCBI_TaxID=1048380 {ECO:0000313|EMBL:GAU77420.1, ECO:0000313|Proteomes:UP000095197};
RN   [1] {ECO:0000313|EMBL:GAU77420.1, ECO:0000313|Proteomes:UP000095197}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3D3 {ECO:0000313|EMBL:GAU77420.1,
RC   ECO:0000313|Proteomes:UP000095197};
RA   Serrano A.E., Escudero L.V., Encalada O., Tebes C.J., Fernandez S.,
RA   Demergasso C.S.;
RT   "Draft genome sequence of Fusibacter ascotence 3D3 isolated from the high
RT   arsenic level Ascotan salt flat in northern Chile.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the transpeptidase family.
CC       {ECO:0000256|ARBA:ARBA00007171}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAU77420.1}.
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DR   EMBL; BDHH01000007; GAU77420.1; -; Genomic_DNA.
DR   RefSeq; WP_069873504.1; NZ_BDHH01000007.1.
DR   AlphaFoldDB; A0A1B6BCG8; -.
DR   STRING; 1048380.F3D3_2049; -.
DR   OrthoDB; 9757901at2; -.
DR   Proteomes; UP000095197; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0008955; F:peptidoglycan glycosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
DR   Gene3D; 3.90.1310.10; Penicillin-binding protein 2a (Domain 2); 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
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   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 2.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 2.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000313|EMBL:GAU77420.1};
KW   Cell division {ECO:0000313|EMBL:GAU77420.1};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Glycosyltransferase {ECO:0000313|EMBL:GAU77420.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095197};
KW   Transferase {ECO:0000313|EMBL:GAU77420.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          52..352
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          420..601
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   DOMAIN          685..789
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   COILED          826..853
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   949 AA;  107831 MW;  BB79F3B27448A87A CRC64;
     MLKLIFNRKN QIIIFFVIVF SLLGYRLYML TIVDGEMYYS KSINNRIKQI ETYAKRGDIY
     DRNGEVLATS NVGFVLKLNS GVIPAEDFTT YAIGLYDFLE EAEESHIEFP IIFKNGEYRY
     VYDDNIKKWK EVNGYDQSMT AADIFREVRS RNYLDTSLSD YEAFKILYNQ GKYVPISTSK
     MKFLDEIYKS TFLKMYGVDE GATAKEAFER IRKRTDFKIS AELPDEDAYK VLVFRHAIKE
     KGYYKYEPIV IAPSIKHETT VKIQEKGFEF PGTSVSYESI RTYPNGSTAA HILGYMGKIS
     TESETSKFVT QNKYNPNQVI GKVGIEGNYE LDLHGENGYK YIEVDVYGKY VQDVDEKAYG
     LEAKNATSGD EIYLTIDLSL QKTLEASLEK ALKGIQKGGK FESPWGDYDY GDAFPQAETG
     AAVAVNVNTG EILAMASYPS YDINLFSTGI SQEDWNSLNP VNTRNPLAAR PLFNTATMMA
     TQPGSIYKMI TGFAAMEQGL DPYLKLYDNG YVEVGNQRYA CWMWNDYRAR HGLVDMLRAI
     EVSCNYYFFD VATGKDFYKN KPLNYTITPQ IIVDESKKFG LDEPTGIEIG ESSFGIPDPD
     KKKRTIKILL SRHLKNISKN YFSDDISKDP EKLQAVIDEI VSWADENPSR GDIIQKLIDM
     GANSDYYVTE KLADIIKYDY FNLMKWYEGD TLNLSIGQGD HTYTPVQMAR YIAALANGGY
     LKELSVVKKV GDESIVKNRE EQVSFDTHGY IDILQEGMLR VSKGSEGTAR KIFGTFPIDV
     AAKTGTAEKE GLIPPLDEIQ YLSEYLSAFA PRLELADVEN RTIEIIKERS EELSKLEKSK
     DEETDEAIRL EKEEKLNLLI ARDYLNKGDA MRAAIKELSG DMLTDEEINQ YRLPYDNYSW
     FVSFAPFDDP ELAVVVVIPQ GGHGAYGAPV ARDVFADYFK LSVPEEPEK
//
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