ID A9E3P1_9FLAO Unreviewed; 433 AA.
AC A9E3P1;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE SubName: Full=Cyanophycinase and related exopeptidase-like protein {ECO:0000313|EMBL:EDP95247.1};
GN ORFNames=KAOT1_09251 {ECO:0000313|EMBL:EDP95247.1};
OS Kordia algicida OT-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Kordia.
OX NCBI_TaxID=391587 {ECO:0000313|EMBL:EDP95247.1, ECO:0000313|Proteomes:UP000002945};
RN [1] {ECO:0000313|EMBL:EDP95247.1, ECO:0000313|Proteomes:UP000002945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT-1 {ECO:0000313|EMBL:EDP95247.1,
RC ECO:0000313|Proteomes:UP000002945};
RX PubMed=21622754; DOI=10.1128/JB.05241-11;
RA Lee H.S., Kang S.G., Kwon K.K., Lee J.H., Kim S.J.;
RT "Genome sequence of the algicidal bacterium Kordia algicida OT-1.";
RL J. Bacteriol. 193:4031-4032(2011).
CC -!- SIMILARITY: Belongs to the peptidase S51 family.
CC {ECO:0000256|ARBA:ARBA00006534}.
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:EDP95247.1}.
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DR EMBL; ABIB01000009; EDP95247.1; -; Genomic_DNA.
DR RefSeq; WP_007094412.1; NZ_DS544873.1.
DR AlphaFoldDB; A9E3P1; -.
DR STRING; 391587.KAOT1_09251; -.
DR MEROPS; S51.003; -.
DR eggNOG; COG4242; Bacteria.
DR HOGENOM; CLU_051822_1_0_10; -.
DR OrthoDB; 9799980at2; -.
DR Proteomes; UP000002945; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd03145; GAT1_cyanophycinase; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR005320; Peptidase_S51.
DR InterPro; IPR026444; Secre_tail.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR PANTHER; PTHR36175; CYANOPHYCINASE; 1.
DR PANTHER; PTHR36175:SF1; CYANOPHYCINASE; 1.
DR Pfam; PF03575; Peptidase_S51; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000002945};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..433
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002737038"
FT DOMAIN 363..432
FT /note="Secretion system C-terminal sorting"
FT /evidence="ECO:0000259|Pfam:PF18962"
SQ SEQUENCE 433 AA; 47156 MW; E5E16A20B434987C CRC64;
MKTYTTILLS FLFAGATFAQ SFTSYRTGSS FSTNVTPQGG SCLMGGASES DDAMRWFLQR
ANGGDVLVLR ASGSDGYNNY MYSDLGVTVN SVETIVFNNS SASSETYIHQ RIEEAEAIWF
AGGDQWNYVS YWRNTTIQNL INDAVNNRNV VIGGTSAGMA ILGGHYFSAE NGTITSAQAL
ANPYANDATV SSTPFLENSF LTDVITDTHY DDPDRRGRHT AFLARIITDN SGSGIIPKGI
ACDEYTAVCI DDVGLARVFG DYPTYDDNAY FIQPNCELTD MLPETCTANT ALHWDKGGMA
LKVYKIKGTV EGTHTFDLSD WQTGTGGTWE HWSVNNGTFV ASVGTQINCI LSVDELAQPT
VEVYPNPVKS NLIVSAEKPI QAIELLDGFG RIVLQKDVSN VQETSLQLLK LSSGTYFLKV
QVNDAIIIKK VIK
//
