ID E5CYR2_CHLTH Unreviewed; 1029 AA.
AC E5CYR2;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Penicillin binding protein {ECO:0000313|EMBL:ADJ67942.1};
DE Flags: Fragment;
GN Name=pbpB {ECO:0000313|EMBL:ADJ67942.1};
OS Chlamydia trachomatis.
OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=813 {ECO:0000313|EMBL:ADJ67942.1};
RN [1] {ECO:0000313|EMBL:ADJ67942.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PbpB_18 {ECO:0000313|EMBL:ADJ67942.1};
RX PubMed=17329456; DOI=10.1128/JCM.02301-06;
RA Klint M., Fuxelius H.H., Goldkuhl R.R., Skarin H., Rutemark C.,
RA Andersson S.G., Persson K., Herrmann B.;
RT "High-resolution genotyping of Chlamydia trachomatis strains by multilocus
RT sequence analysis.";
RL J. Clin. Microbiol. 45:1410-1414(2007).
RN [2] {ECO:0000313|EMBL:ADJ67942.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PbpB_18 {ECO:0000313|EMBL:ADJ67942.1};
RA Herrmann B., Klint M., Christerson L.;
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; GQ352772; ADJ67942.1; -; Genomic_DNA.
DR AlphaFoldDB; E5CYR2; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 2.
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:SF2; PEPTIDOGLYCAN D,D-TRANSPEPTIDASE MRDA; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 2.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 2.
DR SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136}.
FT DOMAIN 24..252
FT /note="Penicillin-binding protein dimerisation"
FT /evidence="ECO:0000259|Pfam:PF03717"
FT DOMAIN 312..340
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT DOMAIN 798..1016
FT /note="Penicillin-binding protein transpeptidase"
FT /evidence="ECO:0000259|Pfam:PF00905"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADJ67942.1"
FT NON_TER 1029
FT /evidence="ECO:0000313|EMBL:ADJ67942.1"
SQ SEQUENCE 1029 AA; 118006 MW; CCF9E0F84FAF4963 CRC64;
VQHEKKKEEA YRPQRRSVPE HCDRAGVCDR FGKTLAENVL QYNVGISYRA IRDIPTRVWH
TDEQGNKRLV PVRKDYIKKF ADFLAQELHM DRDFVEDTIH AKASVLGSVP YILQANVSER
TFLRLKMLEK DWPGLHVESS VRRHYPEGRT VADLLGYVGP ISAEEHRKIT RELGNLRECI
RAYEEGEDPK FPAGISSVDQ VRKLLHELEM HAYGLNSLIG KLGVEAFCDR KLRGLIGKRS
MLVDRRGNFI QEMEGSSVGS PGRKIQLTIS TELQAFAHEL LAEHERGEAF RDYRQWRQQQ
YLPPFFPWIK GGAIVAMDPK NGQILAMASS PRYDNNDFIN MKDSPNQEEC RSSVLRWLEN
LEYIGEVFDR RVPLRRERLD PLSGKYFDEE LSFSYRAFLD FILPDTSKVK QMLCEKGSVG
LSIYLQGTIE QLLEMFECEE KECGLVFDVL FPKEDGHEII GEVTSLKRQK QFKAILAERE
EEVQAFRERL GSIFADLSAN YDKILFLDLL RTAVDPEKVS ISLLAEIGHM SVLDFVDYQG
HFIALRKSFA KLMENAFIDH DFTAWREEHF TQFIKQKRDE ELERKQQYPT PYVDYLVEER
SRQYALFCRE HMDSFITFLL SEIEPPLGNP YYQEIACWRQ ELRSGAYPAL EWREHYDFLH
KHLSQTSYDL CELFAAFREF SELKRPLYGQ YPLTLTRNIE QIEQDLIASF YPLYGYGHLS
AHAFGQAATL GSIFKLVSAY SVLVQHLSDQ EDLSKLLVIV DKQSLGLRSG KPHVGFFKDG
SPIASFFKGG ILPGNDYSGR GYIDLIAALE MSSNPYFSLL VSEYLSDPEN LCEAAKLFGF
GEKTGIGLPG EYAGRVPIDV AYNRSGLYAT AIGQHTLVVT PLQTAVMMAT LVNGGIVYQP
SLIQGEWYQG SFSPEQAKKK REIFLPDSIV DLFKRGMHNV IWGQYGTTRF MRQRFAPERL
ARIIGKTSTA EVIARVGLDR ERGRMKLKDV WFAAVGYEDE ALSHPDIVVV VYLRLGEFGR
DAAPMAVRI
//
