ID   Q97JM7_CLOAB            Unreviewed;       916 AA.
AC   Q97JM7;
DT   01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2001, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   SubName: Full=Penicillin-binding protein 2 {ECO:0000313|EMBL:AAK79218.1};
GN   Name=pbpA {ECO:0000313|EMBL:AAK79218.1};
GN   OrderedLocusNames=CA_C1246 {ECO:0000313|EMBL:AAK79218.1};
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562 {ECO:0000313|EMBL:AAK79218.1, ECO:0000313|Proteomes:UP000000814};
RN   [1] {ECO:0000313|EMBL:AAK79218.1, ECO:0000313|Proteomes:UP000000814}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
RC   {ECO:0000313|Proteomes:UP000000814};
RX   PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
RA   Nolling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC   -!- SIMILARITY: Belongs to the transpeptidase family.
CC       {ECO:0000256|ARBA:ARBA00007171}.
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DR   EMBL; AE001437; AAK79218.1; -; Genomic_DNA.
DR   PIR; G97053; G97053.
DR   RefSeq; NP_347878.1; NC_003030.1.
DR   RefSeq; WP_010964559.1; NC_003030.1.
DR   AlphaFoldDB; Q97JM7; -.
DR   STRING; 272562.CA_C1246; -.
DR   GeneID; 44997753; -.
DR   KEGG; cac:CA_C1246; -.
DR   PATRIC; fig|272562.8.peg.1446; -.
DR   eggNOG; COG0768; Bacteria.
DR   HOGENOM; CLU_009289_1_1_9; -.
DR   OrthoDB; 9757901at2; -.
DR   Proteomes; UP000000814; Chromosome.
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   Gene3D; 1.10.10.1230; Penicillin-binding protein, N-terminal non-catalytic domain, head sub-domain; 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; 1.
DR   SUPFAM; SSF56519; Penicillin binding protein dimerisation domain; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000814}.
FT   DOMAIN          58..347
FT                   /note="Penicillin-binding protein dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF03717"
FT   DOMAIN          403..604
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
FT   DOMAIN          730..876
FT                   /note="Penicillin-binding protein transpeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF00905"
SQ   SEQUENCE   916 AA;  100530 MW;  8145019EC0CD6BBC CRC64;
     MKKSAKFKKI FNRVNVLKVV VLIVFIGITV QLVNLQILQN ANYKAKANNT AHRFIKEVAP
     RGEITDSEGA ILATNKQSFD VTYTQTDDNK DDFYDIIAKV FYILDKNGEK QNDSFALKAD
     SNGYRFDFNT DNCDEIKKMQ IRFLKDRGFE EPIIKKLYKG KSKESDLTDS EVVRVNNELL
     KISPKEVFET LTKKYEIPKA YKISIDGQTI SKNCDVNDIR RFMVVKDAVL IVNGYSGYKP
     VAIASNVKQE TSFTILQKSN ELPGIDISVD PIRDYPYGKL ASNVLGYISK ITPSSSKQSE
     NYTEKGYDVN SDLIGASGIE AALEDRLRGT SGGRIVEVNK QGKITDELAK KDPYPGQNVK
     LTINKDVQYA AEQSLINTMA SLRAKGYSDS NSGSSYLGNA TRGAAVAIDV KTGGVLALAS
     VPNFNPNDFS DPNGLSKEAT EKYFSTDIIS KAKQVGVPES LYDTLFPVSK SDNRTRIDKY
     DYLAKPLYNY ATLSLIPPGS TFKPLTAIAG LETGVITKDT TIDDEGFFDD GKGYRTPFKA
     DGPQGNNNLI GAIAKSSNAY FMTVGKRLRD AYGSDILAKY AWKFGLGVPP NSNITRTTGI
     EVQENFGQVY NTYTIKNSFA DEGQWSIAEK LQEGKYLKGS SVNLYTEDSD SKKLSTLKAS
     IKENIRTAIS TGKTDRNKTE ELVTDLISTD PLYKGKTFSK SDVSALASGI VYDEADEYTQ
     ATVPGNIYNA SIGQGINEFT PLQLANYVAT IANGGKRYKV HLVDKVTDSS GKVVYENKPE
     VVEDTGVSKA NIEAVKEGMN AVNDRGTAAG TFSEFPIPAA GKTGTADPYT SDVERSIMRS
     SYAVYVGFAP RDNPEIAIAT VVFDGGFGNG ITQIGKSMYE AYFKDVLKQK YNFNFDTDVN
     AKPETDAITQ ASNNSN
//