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Database: UniProt
Entry: A0A2T1CVC3_9CYAN
LinkDB: A0A2T1CVC3_9CYAN
Original site: A0A2T1CVC3_9CYAN 
ID   A0A2T1CVC3_9CYAN        Unreviewed;       642 AA.
AC   A0A2T1CVC3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=Cell division protein FtsI {ECO:0000313|EMBL:PSB12200.1};
GN   ORFNames=C7B62_02880 {ECO:0000313|EMBL:PSB12200.1};
OS   Pleurocapsa sp. CCALA 161.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Hyellaceae;
OC   Pleurocapsa.
OX   NCBI_TaxID=2107688 {ECO:0000313|EMBL:PSB12200.1, ECO:0000313|Proteomes:UP000239836};
RN   [1] {ECO:0000313|EMBL:PSB12200.1, ECO:0000313|Proteomes:UP000239836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCALA 161 {ECO:0000313|EMBL:PSB12200.1,
RC   ECO:0000313|Proteomes:UP000239836};
RA   Cohen D.B., Kent A.D.;
RL   Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PSB12200.1, ECO:0000313|Proteomes:UP000239836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCALA 161 {ECO:0000313|EMBL:PSB12200.1,
RC   ECO:0000313|Proteomes:UP000239836};
RA   Moore K.R., Magnabosco C., Momper L., Gold D.A., Bosak T., Fournier G.P.;
RT   "The ancient ancestry and fast evolution of plastids.";
RL   Submitted (MAR-2018) 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:PSB12200.1}.
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DR   EMBL; PVWF01000006; PSB12200.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T1CVC3; -.
DR   InParanoid; A0A2T1CVC3; -.
DR   OrthoDB; 9770103at2; -.
DR   Proteomes; UP000239836; 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:PSB12200.1};
KW   Cell division {ECO:0000313|EMBL:PSB12200.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000239836};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        50..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          110..227
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          309..621
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   642 AA;  71949 MW;  DDBB5869D920264E CRC64;
     MSKSKFKLPF KSNSRNSLKP TKRQQPQRRP SSRNGRNSDW ERTMPTANTA IARLFIIWGI
     LVIGAFALGA KLYYLQVIDP AIKYEQAPQG KKLSQIATDQ QTTKLNFYIP RRQIVDRQQN
     VLATDRITYT LYVHPHLFRR NSQAVPAAEI AEQLSAILGK QTPAELLAIF AKQDWGILLS
     KDLPESVKEK IVGMQIDGLD LKQNYTRFYP HQDMAAEVTG YVNLDSTRTP QAGVEYTQNK
     LLERKPISWK MTRSFENSKS IFHPGNLERS QQLFNFDDLR LQLTIDLRLQ QIARNALKVQ
     MDKYKARKGA VIVMDVRDGA IAALVSEPTY NPNTYYKSKI ELFKNWAITD LYEPGSTFKP
     INLALALDAG VIDPDDTFND TGEIKIKDAL VRNHDFATEG ARGKLTLAEI LKYSSNVGMI
     KIIQRMKPLD YYHDLQKLGI EDQIDFDIPG YTPGRLKNEV EFTVREIEPA TTSFGQGFSL
     TPLKLIQLHA AIANQGKLIT PHVVRGLSDY KGYLHYSQPP NSKQIFSPKT AKTVLEMMEE
     VVEDGSGYAA KIKGYRIAGK TGTSQKAVGQ GGYDDKAKIT SFVGIFPVEA PRYAVLAVVD
     EPHGKYTFGS TVAAPIVGSV IQSIINMEGI PPSNVYHKAA NP
//
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