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Database: UniProt
Entry: O84272_CHLTR
LinkDB: O84272_CHLTR
Original site: O84272_CHLTR 
ID   O84272_CHLTR            Unreviewed;       647 AA.
AC   O84272;
DT   01-NOV-1998, integrated into UniProtKB/TrEMBL.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   SubName: Full=Transglycolase/transpeptidase {ECO:0000313|EMBL:AAC67863.1};
GN   Name=pbp3 {ECO:0000313|EMBL:AAC67863.1};
GN   OrderedLocusNames=CT_270 {ECO:0000313|EMBL:AAC67863.1};
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561 {ECO:0000313|EMBL:AAC67863.1, ECO:0000313|Proteomes:UP000000431};
RN   [1] {ECO:0000313|EMBL:AAC67863.1, ECO:0000313|Proteomes:UP000000431}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx {ECO:0000313|Proteomes:UP000000431};
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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DR   EMBL; AE001273; AAC67863.1; -; Genomic_DNA.
DR   PIR; C71534; C71534.
DR   RefSeq; NP_219775.1; NC_000117.1.
DR   RefSeq; WP_010725146.1; NC_000117.1.
DR   AlphaFoldDB; O84272; -.
DR   STRING; 272561.CT_270; -.
DR   EnsemblBacteria; AAC67863; AAC67863; CT_270.
DR   GeneID; 884853; -.
DR   KEGG; ctr:CT_270; -.
DR   PATRIC; fig|272561.5.peg.289; -.
DR   HOGENOM; CLU_009289_6_4_0; -.
DR   InParanoid; O84272; -.
DR   OrthoDB; 9804124at2; -.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0008658; F:penicillin binding; IBA:GO_Central.
DR   GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
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; 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; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000431};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          267..611
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   647 AA;  73428 MW;  408D14A0CF1117C0 CRC64;
     MNHRRQLTLI VVGVLSLYAL LIVRYYKIQI CDGERWAVEA ANQHEFRVKD PFQRGTFFAN
     TSLRKGEKEQ FHPLAIDVTK FHLCLDAVVI PEEYRDEIAR MVVVMVGEGD YQSIRSEFDR
     KSRYRKLYVS LDISIRDRIL SWWKPYAVKH KIPSNALFFI SDYQRSYPFG KLLGQVLHTL
     REIKDEKSGE AFPTGGLEAY FNRLLEGENG ERKLLRSPLN RLDVDKVTKI PRDGSDIYLT
     IDANVQTIAE QEIALGVLEA KARSGRAIVL NSHTGEILAL AQYPFFNPRE YREYFNCNDR
     IEDTKVKAVS DVFEPGSIMK PITVAIALLA NEEMQKRAGE NLFDPYEPLD VSRRVFPGRQ
     KMPLKDIVSN RYLNMYMAIQ KSSNVYMAQL ADRIVQKLGA DWYEQRLQDF GFGKRTGIEL
     PAEAVGLVPS RKRFHKNGSP EWSLSTPYSL AMGYNLLATS MQMVQAYAVF GNGGFLIRPT
     LVRKIVSPSG EEKILSSNPK KIRVLSEKIV ADVVRAMRFT TCLGGTGIRA ATKGYSSAGK
     TGTTEKLVDG KYDKKRHIAS FIGLTPIAAL SDTAVPLVIL VSIDDPAYGV REDRTKNYMG
     GRCAAPVFSR IASRVLPYLG VPLDEQLHTY REEVSQLKLL YEEWNRK
//
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