ID K9VW32_9CYAN Unreviewed; 511 AA.
AC K9VW32;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Penicillin-binding protein transpeptidase {ECO:0000313|EMBL:AFZ12171.1};
GN ORFNames=Cri9333_1271 {ECO:0000313|EMBL:AFZ12171.1};
OS Crinalium epipsammum PCC 9333.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Gomontiellales; Gomontiellaceae;
OC Crinalium.
OX NCBI_TaxID=1173022 {ECO:0000313|EMBL:AFZ12171.1, ECO:0000313|Proteomes:UP000010472};
RN [1] {ECO:0000313|EMBL:AFZ12171.1, ECO:0000313|Proteomes:UP000010472}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 9333 {ECO:0000313|EMBL:AFZ12171.1,
RC ECO:0000313|Proteomes:UP000010472};
RG US DOE Joint Genome Institute;
RA Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA Pitluck S., Woyke T., Kerfeld C.;
RT "Finished chromosome of genome of Crinalium epipsammum PCC 9333.";
RL Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP003620; AFZ12171.1; -; Genomic_DNA.
DR AlphaFoldDB; K9VW32; -.
DR STRING; 1173022.Cri9333_1271; -.
DR KEGG; cep:Cri9333_1271; -.
DR PATRIC; fig|1173022.3.peg.1377; -.
DR eggNOG; COG2367; Bacteria.
DR HOGENOM; CLU_031960_1_0_3; -.
DR Proteomes; UP000010472; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:InterPro.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR045155; Beta-lactam_cat.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF4; SLR0121 PROTEIN; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000010472};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 165..187
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 244..454
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT REGION 1..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 55668 MW; 225F77AE86F23FCD CRC64;
MAQKRGTKSK LLLISSSNEK LTSNSSKGNL YMSRRQPRDQ PKKASRQEPA KTPTTLQPPQ
QVRQFPTNQG SRNLYAVPVS RQAKTNNSDK IRTVPTSLNQ RLTDTKKIQT AKRRPSLLKF
LSARSTTPRK KPLDLNPRPK ATNHQRQPKG KLGRSQPRPL SPLMYLTRLL IVGVGIGAIV
GTFLSIWDSS SRHSVEAAAN TNSTVEATPA EKKNTITVAM GQEIVAIKPQ LEALATANPK
LQAGVFVLDL DTGAYLDYNS SSTFSAASTI KVPVLVAFFQ DVDAGKVSLD EMLTMEPEMI
AKGSGDMQYQ KAGKQFTALE TATKMIAISD NTATNMLITR LGGAEALNQR FRSWGLVATT
INKPLPDLEG NNSTSPQELA NVMVMVNEGR LVSVRSRDRI LDIMRQTVTK TLLPPGLGKG
ATIAHKTGDI GSILADVGLI DMPIGKRYVA SVMVQRPHND VAARKLIQQI SRLTYQYFDK
SAVSPITPAI PESTPNSMTR AFTGENPAPS N
//
