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Database: UniProt
Entry: F9ZMG4_ACICS
LinkDB: F9ZMG4_ACICS
Original site: F9ZMG4_ACICS 
ID   F9ZMG4_ACICS            Unreviewed;       584 AA.
AC   F9ZMG4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Cell division protein FtsI (Peptidoglycan synthetase) {ECO:0000313|EMBL:AEK57313.1};
GN   OrderedLocusNames=Atc_0664 {ECO:0000313|EMBL:AEK57313.1};
OS   Acidithiobacillus caldus (strain SM-1).
OC   Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=990288 {ECO:0000313|EMBL:AEK57313.1, ECO:0000313|Proteomes:UP000006135};
RN   [1] {ECO:0000313|EMBL:AEK57313.1, ECO:0000313|Proteomes:UP000006135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM-1 {ECO:0000313|EMBL:AEK57313.1,
RC   ECO:0000313|Proteomes:UP000006135};
RX   PubMed=21703548; DOI=10.1016/j.jgg.2011.04.006;
RA   You X.Y., Guo X., Zheng H.J., Zhang M.J., Liu L.J., Zhu Y.Q., Zhu B.,
RA   Wang S.Y., Zhao G.P., Poetsch A., Jiang C.Y., Liu S.J.;
RT   "Unraveling the Acidithiobacillus caldus complete genome and its central
RT   metabolisms for carbon assimilation.";
RL   J. Genet. Genomics 38:243-252(2011).
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DR   EMBL; CP002573; AEK57313.1; -; Genomic_DNA.
DR   RefSeq; WP_004870858.1; NC_015850.1.
DR   AlphaFoldDB; F9ZMG4; -.
DR   STRING; 990288.Atc_0664; -.
DR   GeneID; 69613797; -.
DR   KEGG; acu:Atc_0664; -.
DR   HOGENOM; CLU_009289_6_2_6; -.
DR   OrthoDB; 9766847at2; -.
DR   Proteomes; UP000006135; Chromosome.
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:AEK57313.1};
KW   Cell division {ECO:0000313|EMBL:AEK57313.1};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006135};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          60..207
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          248..544
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   584 AA;  62524 MW;  6C113BF4A52E20E4 CRC64;
     MSKDPRNFQR KLPGWRAAAL FAVIALAFAA VLARDAEVQG WLSQRLRSQG AIRMIQERPL
     PAQRGSILAD NGQALAVNVP AVTVWADPRI FSREKAEWPR VAQVLGLTPA ELAERVKAGG
     ADFAYLERQV LPQLGREISA LHVPGLYVQK TSRSYYPLGP VTTALIGLVH LDHHGAAGLE
     RGYDSWLSGQ PGREKVLVDG KGEVLRVLGR PRPPVNGHDL HLTIDPQIQY WAYMTLRAAQ
     KHFGAENGSA VVMNVHSGQI LAMVSVPSCN PNTRDGCTNP SDYVNNAVHQ AFEPGSVMKP
     FMVAAALATG SIRPDQRFDV AHCLPVGGFC IRDDVVHREL DVAHILKYSS DVGAAKIALR
     TPAEAIAQMY RAAGFGEPAP LGFDEATAGV LPPAQSWDRA RHATIALGYG VSVTTLQLAE
     GYAAIANGGY HVQPVLVAGQ TGQSRRIMPA AIADRLRHWL EGVCAANGTG ILAAIPGYSV
     AGKTGTANLA NGKGGFNKKK TNATFVGFAP GFAPDLVMAV SLRGSTRYWN FGGVESAPVF
     RVTMRHALQR LDIAPRWCGS RACVSKDANV TTTQAEIWAE GGGK
//
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