ID   FTSIH_CHLAT             Reviewed;         679 AA.
AC   A2CI41;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Peptidoglycan D,D-transpeptidase FtsI homolog {ECO:0000305};
DE            EC=3.4.16.4 {ECO:0000250|UniProtKB:P0AD68};
GN   Name=ftsI;
OS   Chlorokybus atmophyticus (Soil alga).
OG   Plastid; Chloroplast.
OC   Eukaryota; Viridiplantae; Streptophyta; Chlorokybophyceae; Chlorokybales;
OC   Chlorokybaceae; Chlorokybus.
OX   NCBI_TaxID=3144;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAG 48.80;
RX   PubMed=17222354; DOI=10.1186/1741-7007-5-2;
RA   Lemieux C., Otis C., Turmel M.;
RT   "A clade uniting the green algae Mesostigma viride and Chlorokybus
RT   atmophyticus represents the deepest branch of the Streptophyta in
RT   chloroplast genome-based phylogenies.";
RL   BMC Biol. 5:2-2(2007).
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;
CC         Evidence={ECO:0000250|UniProtKB:P0AD68};
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast membrane {ECO:0000305};
CC       Single-pass membrane protein {ECO:0000305}.
CC   -!- MISCELLANEOUS: The presence of this gene in the chloroplast genome
CC       suggests there may be an unsuspected vestigal peptidoglycan layer in
CC       this organism's chloroplasts.
CC   -!- SIMILARITY: Belongs to the transpeptidase family. {ECO:0000305}.
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DR   EMBL; DQ422812; ABM87954.1; -; Genomic_DNA.
DR   RefSeq; YP_001019071.1; NC_008822.1.
DR   AlphaFoldDB; A2CI41; -.
DR   SMR; A2CI41; -.
DR   GeneID; 4783320; -.
DR   GO; GO:0031969; C:chloroplast membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0009002; F:serine-type D-Ala-D-Ala carboxypeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.710.10; -; 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   Pfam; PF03717; PBP_dimer; 1.
DR   Pfam; PF00905; Transpeptidase; 2.
DR   SUPFAM; SSF56519; SSF56519; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase; Cell shape; Chloroplast; Hydrolase; Membrane;
KW   Peptidoglycan synthesis; Plastid; Protease; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..679
FT                   /note="Peptidoglycan D,D-transpeptidase FtsI homolog"
FT                   /id="PRO_0000314459"
FT   TRANSMEM        13..33
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        292
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P0AD68"
SQ   SEQUENCE   679 AA;  75878 MW;  55BEB81500C9F33E CRC64;
     MKPYEPKSWV TRVFLVWWLT ALSCFFISGR LIYLQLLKGK WLKEKALKQQ TVTLKTFQPR
     RNICDRNGIP LAIDTLAYDV FAHPLYFSIS IEEVANKLSP ILCIDSLSIQ KLLKPTSTGI
     CLASQLPENT GKLIASLRLD GIDLIKHPKR YYPYKEIVGN VIGYVDTSHQ GQAGIELSCQ
     ESLQLNSPTL TSSIDGRGVL ISHQIPKELF IQDNLSLQLT LDLELQKIAY KALKQGLENC
     KGKRGTVLIL DPKTGGILTL VALPSYDPNI YYDFPIERFK PWPVTDLYEP GSTFKPLNIA
     IALETKAISP EDSFYDEGCI RVGDSIITNN DYNSYKPLPC LPNTYNKIVK LLANSSNVGM
     VHILERIAPE IYHSWLSKLD LGHAASPLET DLPWASESSL KDINEFVCYE IEPAAASFGQ
     GLAMTPIKLA QLYASLANGG ILVKPYLVTG LANAAEDTQK AKGIDLPSYN IRKKNLGNHL
     SWHKAEPSYL FLKRSGIRVT DLLRHIKAEG RFALPFRKNL LQLFTQDAHR TTELQLEPKA
     HQPQLLRPTR HAVYATNQSK RVFSHETTKL LLDMLEDVIW NGTGSSCFVE GYRIGGKTGT
     SQKHTQEGGY SKTKIITSFA AIFPTEDPQY VILTVIDEPN IPLSFGSNTA APIVKSIIES
     LIDIKKMKPT IPIIKVKKD