PBPX_STRPN
ID PBPX_STRPN Reviewed; 750 AA.
AC P14677;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Penicillin-binding protein 2x;
DE Short=PBP-2x;
DE Short=PBP2x;
GN Name=pbpX; OrderedLocusNames=SP_0336;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF 76-750.
RX PubMed=8605631; DOI=10.1038/nsb0396-284;
RA Pares S., Mouz N., Petillot Y., Hakenbeck R., Dideberg O.;
RT "X-ray structure of Streptococcus pneumoniae PBP2x, a primary penicillin
RT target enzyme.";
RL Nat. Struct. Biol. 3:284-289(1996).
CC -!- FUNCTION: A transpeptidase that forms peptide cross-links between
CC adjacent glycan strands in cell wall peptidoglycan (PG). Part of the
CC divisome machinery that synthesizes the septal cross wall. Beta-lactams
CC inactivate the PBPs by acylating an essential serine residue in the
CC active site of these proteins. {ECO:0000250|UniProtKB:P59676}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC -!- MISCELLANEOUS: The mature form of PBP2x contains an unprocessed signal
CC sequence followed by a membrane-anchoring segment.
CC -!- SIMILARITY: Belongs to the transpeptidase family. {ECO:0000305}.
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DR EMBL; AE005672; AAK74511.1; -; Genomic_DNA.
DR PIR; F95039; F95039.
DR PIR; H97909; H97909.
DR PIR; S06726; S06726.
DR RefSeq; WP_000872275.1; NZ_AKVY01000001.1.
DR PDB; 1PMD; X-ray; 3.50 A; A=76-750.
DR PDB; 1QME; X-ray; 2.40 A; A=49-750.
DR PDB; 1QMF; X-ray; 2.80 A; A=49-750.
DR PDB; 1RP5; X-ray; 3.00 A; A/B=49-750.
DR PDB; 2Z2L; X-ray; 2.85 A; A/D=71-238, B/E=241-625, C/F=626-750.
DR PDB; 2Z2M; X-ray; 2.60 A; A/D=71-238, B/E=241-625, C/F=626-750.
DR PDB; 2ZC3; X-ray; 2.50 A; A/D=71-238, B/E=241-625, C/F=626-750.
DR PDB; 2ZC4; X-ray; 2.80 A; A/D=71-238, B/E=241-625, C/F=626-750.
DR PDBsum; 1PMD; -.
DR PDBsum; 1QME; -.
DR PDBsum; 1QMF; -.
DR PDBsum; 1RP5; -.
DR PDBsum; 2Z2L; -.
DR PDBsum; 2Z2M; -.
DR PDBsum; 2ZC3; -.
DR PDBsum; 2ZC4; -.
DR AlphaFoldDB; P14677; -.
DR SMR; P14677; -.
DR STRING; 170187.SP_0336; -.
DR BindingDB; P14677; -.
DR ChEMBL; CHEMBL6188; -.
DR DrugBank; DB01150; Cefprozil.
DR DrugBank; DB04918; Ceftobiprole.
DR EnsemblBacteria; AAK74511; AAK74511; SP_0336.
DR KEGG; spn:SP_0336; -.
DR eggNOG; COG0768; Bacteria.
DR OMA; HGKEEYY; -.
DR PhylomeDB; P14677; -.
DR BioCyc; SPNE170187:G1FZB-345-MON; -.
DR BRENDA; 2.4.1.129; 1960.
DR EvolutionaryTrace; P14677; -.
DR PRO; PR:P14677; -.
DR Proteomes; UP000000585; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR Gene3D; 3.40.710.10; -; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR005543; PASTA_dom.
DR InterPro; IPR005311; PBP_dimer.
DR InterPro; IPR036138; PBP_dimer_sf.
DR InterPro; IPR001460; PCN-bd_Tpept.
DR Pfam; PF03793; PASTA; 1.
DR Pfam; PF03717; PBP_dimer; 1.
DR Pfam; PF00905; Transpeptidase; 1.
DR SMART; SM00740; PASTA; 1.
DR SUPFAM; SSF56519; SSF56519; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
DR PROSITE; PS51178; PASTA; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Cell cycle; Cell division;
KW Cell membrane; Cell shape; Cell wall biogenesis/degradation; Membrane;
KW Peptidoglycan synthesis; Repeat; Transmembrane; Transmembrane helix.
FT CHAIN 1..750
FT /note="Penicillin-binding protein 2x"
FT /id="PRO_0000195453"
FT TRANSMEM 29..49
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 632..691
FT /note="PASTA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT DOMAIN 692..750
FT /note="PASTA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00528"
FT ACT_SITE 337
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0AD65"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:1RP5"
FT STRAND 86..91
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 93..99
FT /evidence="ECO:0007829|PDB:1RP5"
FT STRAND 107..109
FT /evidence="ECO:0007829|PDB:2Z2L"
FT TURN 116..118
FT /evidence="ECO:0007829|PDB:2ZC3"
FT HELIX 119..130
FT /evidence="ECO:0007829|PDB:2ZC3"
FT HELIX 134..141
FT /evidence="ECO:0007829|PDB:2ZC3"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:2ZC3"
FT HELIX 153..155
FT /evidence="ECO:0007829|PDB:2ZC3"
FT STRAND 156..158
FT /evidence="ECO:0007829|PDB:2ZC3"
FT HELIX 160..170
FT /evidence="ECO:0007829|PDB:2ZC3"
FT TURN 171..174
FT /evidence="ECO:0007829|PDB:2ZC3"
FT STRAND 177..183
FT /evidence="ECO:0007829|PDB:1RP5"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:1QME"
FT HELIX 195..198
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:1QME"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:2ZC3"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:1QME"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:1QME"
FT HELIX 224..228
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:1RP5"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:1RP5"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:1QME"
FT HELIX 267..284
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 287..295
FT /evidence="ECO:0007829|PDB:1QME"
FT TURN 296..298
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 300..308
FT /evidence="ECO:0007829|PDB:1QME"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:1QME"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:1QME"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:1QME"
FT HELIX 340..349
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:1QME"
FT HELIX 374..377
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:2Z2L"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:1QME"
FT HELIX 388..393
FT /evidence="ECO:0007829|PDB:1QME"
FT HELIX 397..407
FT /evidence="ECO:0007829|PDB:1QME"
FT HELIX 409..418
FT /evidence="ECO:0007829|PDB:1QME"
FT TURN 419..422
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 428..431
FT /evidence="ECO:0007829|PDB:1QME"
FT HELIX 442..447
FT /evidence="ECO:0007829|PDB:1QME"
FT HELIX 448..450
FT /evidence="ECO:0007829|PDB:1QME"
FT HELIX 458..469
FT /evidence="ECO:0007829|PDB:1QME"
FT TURN 470..472
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 480..485
FT /evidence="ECO:0007829|PDB:1QME"
FT TURN 486..489
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 490..493
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 498..500
FT /evidence="ECO:0007829|PDB:1QME"
FT HELIX 505..520
FT /evidence="ECO:0007829|PDB:1QME"
FT TURN 522..524
FT /evidence="ECO:0007829|PDB:1QME"
FT TURN 530..532
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 533..537
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 545..552
FT /evidence="ECO:0007829|PDB:1QME"
FT HELIX 556..558
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 559..561
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 568..580
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 582..591
FT /evidence="ECO:0007829|PDB:1QME"
FT HELIX 597..617
FT /evidence="ECO:0007829|PDB:1QME"
FT HELIX 625..628
FT /evidence="ECO:0007829|PDB:1RP5"
FT HELIX 646..654
FT /evidence="ECO:0007829|PDB:1QME"
FT TURN 655..657
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 659..665
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 667..674
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 685..691
FT /evidence="ECO:0007829|PDB:1QME"
FT HELIX 704..714
FT /evidence="ECO:0007829|PDB:1QME"
FT STRAND 717..732
FT /evidence="ECO:0007829|PDB:1QME"
FT TURN 738..740
FT /evidence="ECO:0007829|PDB:2ZC3"
FT STRAND 743..749
FT /evidence="ECO:0007829|PDB:1QME"
SQ SEQUENCE 750 AA; 82313 MW; 9B2BCADBE4E462E4 CRC64;
MKWTKRVIRY ATKNRKSPAE NRRRVGKSLS LLSVFVFAIF LVNFAVIIGT GTRFGTDLAK
EAKKVHQTTR TVPAKRGTIY DRNGVPIAED ATSYNVYAVI DENYKSATGK ILYVEKTQFN
KVAEVFHKYL DMEESYVREQ LSQPNLKQVS FGAKGNGITY ANMMSIKKEL EAAEVKGIDF
TTSPNRSYPN GQFASSFIGL AQLHENEDGS KSLLGTSGME SSLNSILAGT DGIITYEKDR
LGNIVPGTEQ VSQRTMDGKD VYTTISSPLQ SFMETQMDAF QEKVKGKYMT ATLVSAKTGE
ILATTQRPTF DADTKEGITE DFVWRDILYQ SNYEPGSTMK VMMLAAAIDN NTFPGGEVFN
SSELKIADAT IRDWDVNEGL TGGRTMTFSQ GFAHSSNVGM TLLEQKMGDA TWLDYLNRFK
FGVPTRFGLT DEYAGQLPAD NIVNIAQSSF GQGISVTQTQ MIRAFTAIAN DGVMLEPKFI
SAIYDPNDQT ARKSQKEIVG NPVSKDAASL TRTNMVLVGT DPVYGTMYNH STGKPTVTVP
GQNVALKSGT AQIADEKNGG YLVGLTDYIF SAVSMSPAEN PDFILYVTVQ QPEHYSGIQL
GEFANPILER ASAMKDSLNL QTTAKALEQV SQQSPYPMPS VKDISPGDLA EELRRNLVQP
IVVGTGTKIK NSSAEEGKNL APNQQVLILS DKAEEVPDMY GWTKETAETL AKWLNIELEF
QGSGSTVQKQ DVRANTAIKD IKKITLTLGD
