ID Q2JM72_SYNJB Unreviewed; 788 AA.
AC Q2JM72;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Putative membrane-bound protease {ECO:0000313|EMBL:ABD02172.1};
GN OrderedLocusNames=CYB_1197 {ECO:0000313|EMBL:ABD02172.1};
OS Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS Yellowstone B-Prime).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=321332 {ECO:0000313|EMBL:ABD02172.1, ECO:0000313|Proteomes:UP000001938};
RN [1] {ECO:0000313|EMBL:ABD02172.1, ECO:0000313|Proteomes:UP000001938}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-2-3B'a(2-13) {ECO:0000313|Proteomes:UP000001938};
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(2007).
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DR EMBL; CP000240; ABD02172.1; -; Genomic_DNA.
DR RefSeq; WP_011432825.1; NC_007776.1.
DR AlphaFoldDB; Q2JM72; -.
DR STRING; 321332.CYB_1197; -.
DR KEGG; cyb:CYB_1197; -.
DR eggNOG; COG1305; Bacteria.
DR HOGENOM; CLU_012397_2_0_3; -.
DR OrthoDB; 9804872at2; -.
DR Proteomes; UP000001938; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.10.620.30; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR021878; TgpA_N.
DR InterPro; IPR002931; Transglutaminase-like.
DR PANTHER; PTHR42736; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
DR PANTHER; PTHR42736:SF1; PROTEIN-GLUTAMINE GAMMA-GLUTAMYLTRANSFERASE; 1.
DR Pfam; PF11992; TgpA_N; 1.
DR Pfam; PF01841; Transglut_core; 1.
DR SMART; SM00460; TGc; 1.
DR SUPFAM; SSF54001; Cysteine proteinases; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ABD02172.1};
KW Membrane {ECO:0000256|SAM:Phobius}; Protease {ECO:0000313|EMBL:ABD02172.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001938};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 69..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 107..127
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 174..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 613..631
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 643..661
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 667..687
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 462..533
FT /note="Transglutaminase-like"
FT /evidence="ECO:0000259|SMART:SM00460"
SQ SEQUENCE 788 AA; 88370 MW; B138F7A5F1ACE068 CRC64;
MTWTLPSVQK VFVYLLVGIA FTALCLGDQA LSPPVIAVCL AAGACSWFWE PPRIAFARYA
PLWMPLTVAV LLSLLALVIF GILPFSDGAI GLVLYLTGAK LFQRERAADH IQLAVLSLLL
MAIATLFNED ISFGLLFLLY VGVGLINLTL YHLRLQAEQH PQAASQTRGI NLNFLGFLGS
LALLAVILSV ALFFLFPRVS LGILGRQARS PVMTTGFAEE VSLGAFGTLK TDNTVVMRVE
FPAGVPPRVE SLYWRGISFD RYDGLAWSRT LDRFIPIFPN AAGVFDLSAS SLIPTAPDLL
LLPLEQLIYL EPLATNTVFG VAPLVEVEWL DRGGAMTPQQ RWQWQNRRLL LRETGDVSHS
LPPRMPYLYR AVSRIPRDLE PRLRQLGREE LLSALDPVQQ QAYLQLPADL DPRIPALAED
VTAGIPDVFG KVTALQNYLL ENYAYTTDLP DPGPEPPLEA FLFTHRRGHC EYFATALTIL
ARSIGIPARM VNGFLGGRWV AQERYLAVRN ADAHSWTEIP FGSYGWIIFD ATPAEANVSR
RETWWDPIQD FYDSLRFRWF KYVIQYDLST QQQIWRQIQE MASAVAASPD REDVGAGFRR
NLVALGQTLQ QNGLPVLGVV LITGSMAYWG RRRRYRALRW QDGGWILLAT AGNGVLLGSL
WQPPPPWPTW MVGLLLPSLA FAGMRWIPAA LPKSQQRRQL ISRLYLQLRD LATAVGIPAH
LGPEACLEHL RHSDLPQAQV AIQFLERYLE VRFGGIPLEA GELQRWQQQF KRLRRAWQPL
AKTPRRAA
//
