PBPB_MYCTU
ID PBPB_MYCTU Reviewed; 679 AA.
AC L0T911;
DT 26-JUN-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 25-MAY-2022, entry version 45.
DE RecName: Full=Penicillin-binding protein PbpB;
DE AltName: Full=Penicillin-binding protein 3;
DE Short=PBP3;
GN Name=pbpB; Synonyms=ftsI, pbp3; OrderedLocusNames=Rv2163c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, TOPOLOGY, INTERACTION WITH
RP WAG31, CLEAVAGE BY RIP1, AND MUTAGENESIS OF ALA-102; ALA-103;
RP 427-HIS--VAL-429 AND 488-GLN--SER-490.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=19496931; DOI=10.1111/j.1365-2958.2009.06750.x;
RA Mukherjee P., Sureka K., Datta P., Hossain T., Barik S., Das K.P.,
RA Kundu M., Basu J.;
RT "Novel role of Wag31 in protection of mycobacteria under oxidative
RT stress.";
RL Mol. Microbiol. 73:103-119(2009).
CC -!- FUNCTION: Synthesis of cross-linked peptidoglycan from the lipid
CC intermediates. {ECO:0000250, ECO:0000269|PubMed:19496931}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis.
CC -!- SUBUNIT: Interacts with Wag31. {ECO:0000269|PubMed:19496931}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The enzyme has an N-terminal penicillin insensitive
CC transglycosylase domain (formation of linear glycan strands) and a C-
CC terminal penicillin-sensitive transpeptidase domain (cross-linking of
CC the peptide subunits). {ECO:0000250}.
CC -!- PTM: Cleaved by Rip1 in response to oxidative stress (H(2)O(2)),
CC prevented by Wag31. Cleavage probably occurs near residues 102-103.
CC -!- SIMILARITY: Belongs to the transpeptidase family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44940.1; -; Genomic_DNA.
DR RefSeq; NP_216679.1; NC_000962.3.
DR RefSeq; WP_003411214.1; NZ_NVQJ01000088.1.
DR PDB; 6KGH; X-ray; 2.11 A; A=123-679.
DR PDB; 6KGS; X-ray; 2.31 A; A=123-679.
DR PDB; 6KGT; X-ray; 2.31 A; A=123-679.
DR PDB; 6KGU; X-ray; 2.11 A; A=123-679.
DR PDB; 6KGV; X-ray; 2.30 A; A=123-679.
DR PDB; 6KGW; X-ray; 2.41 A; A=123-679.
DR PDBsum; 6KGH; -.
DR PDBsum; 6KGS; -.
DR PDBsum; 6KGT; -.
DR PDBsum; 6KGU; -.
DR PDBsum; 6KGV; -.
DR PDBsum; 6KGW; -.
DR AlphaFoldDB; L0T911; -.
DR SMR; L0T911; -.
DR IntAct; L0T911; 1.
DR STRING; 83332.Rv2163c; -.
DR PaxDb; L0T911; -.
DR PRIDE; L0T911; -.
DR DNASU; 887949; -.
DR GeneID; 887949; -.
DR KEGG; mtu:Rv2163c; -.
DR TubercuList; Rv2163c; -.
DR eggNOG; COG0768; Bacteria.
DR InParanoid; L0T911; -.
DR OMA; HGKEEYY; -.
DR PhylomeDB; L0T911; -.
DR UniPathway; UPA00219; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0008658; F:penicillin binding; IBA:GO_Central.
DR GO; GO:0071555; P:cell wall organization; IBA:GO_Central.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-UniPathway.
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; 1.
DR SUPFAM; SSF56519; SSF56519; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell shape; Cell wall biogenesis/degradation;
KW Membrane; Peptidoglycan synthesis; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..679
FT /note="Penicillin-binding protein PbpB"
FT /id="PRO_0000422679"
FT TOPO_DOM 1..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:19496931"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 112..679
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:19496931"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 386
FT /note="Acyl-ester intermediate"
FT /evidence="ECO:0000250|UniProtKB:P0AD65"
FT MUTAGEN 102..103
FT /note="AA->LL: No degradation by Rip1."
FT MUTAGEN 102
FT /note="A->L: No effect on degradation by Rip1."
FT /evidence="ECO:0000269|PubMed:19496931"
FT MUTAGEN 103
FT /note="A->L: No effect on degradation by Rip1."
FT /evidence="ECO:0000269|PubMed:19496931"
FT MUTAGEN 427..429
FT /note="Missing: Decreased interaction with Wag31. Loss of
FT interaction, reduced protection from Rip1 proteolysis; when
FT associated with 488-Q--S-490 deletion."
FT /evidence="ECO:0000269|PubMed:19496931"
FT MUTAGEN 488..490
FT /note="Missing: Decreased interaction with Wag31. Loss of
FT interaction, reduced protection from Rip1 proteolysis; when
FT associated with 427-H--V-429 deletion."
FT /evidence="ECO:0000269|PubMed:19496931"
FT STRAND 145..153
FT /evidence="ECO:0007829|PDB:6KGU"
FT STRAND 239..244
FT /evidence="ECO:0007829|PDB:6KGU"
FT TURN 246..251
FT /evidence="ECO:0007829|PDB:6KGU"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:6KGU"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:6KGU"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:6KGU"
FT HELIX 273..277
FT /evidence="ECO:0007829|PDB:6KGU"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:6KGU"
FT HELIX 316..333
FT /evidence="ECO:0007829|PDB:6KGU"
FT STRAND 336..344
FT /evidence="ECO:0007829|PDB:6KGU"
FT TURN 345..347
FT /evidence="ECO:0007829|PDB:6KGU"
FT STRAND 349..358
FT /evidence="ECO:0007829|PDB:6KGU"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:6KGU"
FT HELIX 376..379
FT /evidence="ECO:0007829|PDB:6KGU"
FT HELIX 385..388
FT /evidence="ECO:0007829|PDB:6KGU"
FT HELIX 389..398
FT /evidence="ECO:0007829|PDB:6KGU"
FT STRAND 412..416
FT /evidence="ECO:0007829|PDB:6KGU"
FT STRAND 419..422
FT /evidence="ECO:0007829|PDB:6KGU"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:6KGU"
FT HELIX 434..440
FT /evidence="ECO:0007829|PDB:6KGU"
FT HELIX 443..453
FT /evidence="ECO:0007829|PDB:6KGU"
FT HELIX 455..464
FT /evidence="ECO:0007829|PDB:6KGU"
FT TURN 465..468
FT /evidence="ECO:0007829|PDB:6KGU"
FT HELIX 486..488
FT /evidence="ECO:0007829|PDB:6KGU"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:6KGU"
FT HELIX 497..499
FT /evidence="ECO:0007829|PDB:6KGU"
FT HELIX 507..518
FT /evidence="ECO:0007829|PDB:6KGU"
FT TURN 519..521
FT /evidence="ECO:0007829|PDB:6KGU"
FT STRAND 529..533
FT /evidence="ECO:0007829|PDB:6KGU"
FT STRAND 539..541
FT /evidence="ECO:0007829|PDB:6KGU"
FT HELIX 553..562
FT /evidence="ECO:0007829|PDB:6KGU"
FT HELIX 563..567
FT /evidence="ECO:0007829|PDB:6KGU"
FT HELIX 580..582
FT /evidence="ECO:0007829|PDB:6KGU"
FT STRAND 590..599
FT /evidence="ECO:0007829|PDB:6KGU"
FT TURN 601..603
FT /evidence="ECO:0007829|PDB:6KGU"
FT STRAND 604..619
FT /evidence="ECO:0007829|PDB:6KGU"
FT STRAND 621..623
FT /evidence="ECO:0007829|PDB:6KGU"
FT STRAND 626..634
FT /evidence="ECO:0007829|PDB:6KGU"
FT STRAND 641..644
FT /evidence="ECO:0007829|PDB:6KGU"
FT HELIX 648..661
FT /evidence="ECO:0007829|PDB:6KGU"
SQ SEQUENCE 679 AA; 72537 MW; 3FE57B17A4D265C4 CRC64;
MSRAAPRRAS QSQSTRPARG LRRPPGAQEV GQRKRPGKTQ KARQAQEATK SRPATRSDVA
PAGRSTRARR TRQVVDVGTR GASFVFRHRT GNAVILVLML VAATQLFFLQ VSHAAGLRAQ
AAGQLKVTDV QPAARGSIVD RNNDRLAFTI EARALTFQPK RIRRQLEEAR KKTSAAPDPQ
QRLRDIAQEV AGKLNNKPDA AAVLKKLQSD ETFVYLARAV DPAVASAICA KYPEVGAERQ
DLRQYPGGSL AANVVGGIDW DGHGLLGLED SLDAVLAGTD GSVTYDRGSD GVVIPGSYRN
RHKAVHGSTV VLTLDNDIQF YVQQQVQQAK NLSGAHNVSA VVLDAKTGEV LAMANDNTFD
PSQDIGRQGD KQLGNPAVSS PFEPGSVNKI VAASAVIEHG LSSPDEVLQV PGSIQMGGVT
VHDAWEHGVM PYTTTGVFGK SSNVGTLMLS QRVGPERYYD MLRKFGLGQR TGVGLPGESA
GLVPPIDQWS GSTFANLPIG QGLSMTLLQM TGMYQAIAND GVRVPPRIIK ATVAPDGSRT
EEPRPDDIRV VSAQTAQTVR QMLRAVVQRD PMGYQQGTGP TAGVPGYQMA GKTGTAQQIN
PGCGCYFDDV YWITFAGIAT ADNPRYVIGI MLDNPARNSD GAPGHSAAPL FHNIAGWLMQ
RENVPLSPDP GPPLVLQAT
