ID A0A139X3L3_9CYAN Unreviewed; 537 AA.
AC A0A139X3L3;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Serine hydrolase {ECO:0000313|EMBL:KYC39264.1};
GN ORFNames=WA1_31480 {ECO:0000313|EMBL:KYC39264.1};
OS Scytonema hofmannii PCC 7110.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC Scytonema.
OX NCBI_TaxID=128403 {ECO:0000313|EMBL:KYC39264.1, ECO:0000313|Proteomes:UP000076925};
RN [1] {ECO:0000313|EMBL:KYC39264.1, ECO:0000313|Proteomes:UP000076925}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7110 {ECO:0000313|EMBL:KYC39264.1,
RC ECO:0000313|Proteomes:UP000076925};
RX PubMed=23221676; DOI=10.1093/gbe/evs117;
RA Dagan T., Roettger M., Stucken K., Landan G., Koch R., Major P.,
RA Gould S.B., Goremykin V.V., Rippka R., Tandeau de Marsac N., Gugger M.,
RA Lockhart P.J., Allen J.F., Brune I., Maus I., Puhler A., Martin W.F.;
RT "Genomes of Stigonematalean cyanobacteria (subsection V) and the evolution
RT of oxygenic photosynthesis from prokaryotes to plastids.";
RL Genome Biol. Evol. 5:31-44(2013).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYC39264.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ANNX02000035; KYC39264.1; -; Genomic_DNA.
DR RefSeq; WP_017740342.1; NZ_KQ976354.1.
DR AlphaFoldDB; A0A139X3L3; -.
DR STRING; 128403.WA1_31480; -.
DR OrthoDB; 9775096at2; -.
DR Proteomes; UP000076925; Unassembled WGS sequence.
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 Hydrolase {ECO:0000313|EMBL:KYC39264.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076925};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 117..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 207..417
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT REGION 21..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 537 AA; 57669 MW; F0F097DC59541A27 CRC64;
MNTRTRIKVI SQRRPDLRKV QKLPQNKMEV HNQQRPPQKK PTSTRVKVIP PLKPATVPRR
QPRGVTPPIN HSATFKGRIP PYNPNTVQLK TAHLQKHPVM KQSYSSRKTR LKPMARTILY
ALRLLIVGVG IGAIVGTVLS VLDPATRLAT PGSVSSDTTV AQKAQSQPTL TPTPTPTATS
LSLSQELIPL KSAVQSLAAS NPNLTPGVFL IDLDNGGYVD LNGAASFAAA STIKIPILVA
FFQDVDAQKI RLDESLTLES GMVAGGSGNM QYKPVGTQFT ALEVATKMMT VSDNTATNML
IARLGGIDAL NQRFQSWGLT TTAIRNILPD LGGTNTTSPK ELSTLMAMVG KGNLVSMRSR
DRILDIMRRT VRNHLLPAGL GPGATIAHKT GNIGTILGDA GLVDVPTGKR YVVSVMVQRP
RNDPGAEKLI TSISRVAYEQ LSQTFPVPNN TGSSIPNTGY QQPPVVSPLP AISPPPAINQ
PLPNGISNTL PLTGYQPPVM NPPLPNGMSN TLPPTGYQAP AIAPQVAPQY YYNPYQR
//
