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Database: UniProt
Entry: A0A0P7XGQ1_9RHOB
LinkDB: A0A0P7XGQ1_9RHOB
Original site: A0A0P7XGQ1_9RHOB 
ID   A0A0P7XGQ1_9RHOB        Unreviewed;       595 AA.
AC   A0A0P7XGQ1;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=Cell division protein (Peptidoglycan synthetase) FtsI {ECO:0000313|EMBL:KPQ06743.1};
GN   Name=ftsI {ECO:0000313|EMBL:KPQ06743.1};
GN   ORFNames=HLUCCA12_09050 {ECO:0000313|EMBL:KPQ06743.1};
OS   Rhodobacteraceae bacterium HLUCCA12.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1666916 {ECO:0000313|EMBL:KPQ06743.1, ECO:0000313|Proteomes:UP000050476};
RN   [1] {ECO:0000313|EMBL:KPQ06743.1, ECO:0000313|Proteomes:UP000050476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HLUCCA12 {ECO:0000313|EMBL:KPQ06743.1};
RA   Nelson W.C., Romine M.F., Lindemann S.R.;
RT   "Identification and resolution of microdiversity through metagenomic
RT   sequencing of parallel consortia.";
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:KPQ06743.1}.
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DR   EMBL; LJSV01000007; KPQ06743.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7XGQ1; -.
DR   STRING; 1666916.HLUCCA12_09050; -.
DR   PATRIC; fig|1666916.3.peg.2731; -.
DR   Proteomes; UP000050476; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; 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   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   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   4: Predicted;
KW   Cell cycle {ECO:0000313|EMBL:KPQ06743.1};
KW   Cell division {ECO:0000313|EMBL:KPQ06743.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        47..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          86..223
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   REGION          278..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   595 AA;  65026 MW;  AF99B65296440EB1 CRC64;
     MIRIPLRPLP RILEARAEGR NPAHIERENL RLRHEQMRDL ARRRAEWRLL FLAALFFMGF
     ALIGARMGLL AASPPHEPMP YQGEEIAAYR AEIQDRNGRI LATNLVTNSL YAEMRYMVDG
     ARAARELARI FPDIDAERLA ARLTDPDRRF VWIRTRLSPE QVQAVHDIGE PGLLFGPREM
     RLYPNGRLAA HVLGGTSFGQ QGVNAAEIVG TGGIEHRLDA TLRDPDRAER PMRLSLDLTV
     QAIAAEVLDG GVSMLGARAG SATVMDARTG EIVAMVSLPD FDPNDRPAPP TEGDPTDSPL
     FNHAVQGVYE LGSVMKAFGV AQALELDLVT PETMIDTRAP LRIGGHAIND FRNYGAEMSV
     RDVFVRSSNI GTARLAQMIG ADRQRDFLQR FGFLEPASVE LAETARARPQ FPDRWTEISS
     MTISYGHGLS TSPLQLAAAY AALVNGGTRV EPTLLRRATA APGERLISER TSAMMRALMR
     QVVTTGTASM AEVEGFVFGG KTGTADKPDP SGGYAEDRVI ATFAGAFPLD DPRYVVVITL
     DEPNETSSGE ARRTAGWTVV PVAAEIVRRT APLLGLRPRD DARATAAIEA ALQLR
//
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