ID A0A1Y5JNM9_9GAMM Unreviewed; 795 AA.
AC A0A1Y5JNM9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Peptidase C-terminal archaeal/bacterial domain-containing protein {ECO:0000259|Pfam:PF04151};
GN ORFNames=B5G52_20715 {ECO:0000313|EMBL:OUS67973.1};
OS Pseudoalteromonas sp. A601.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1967839 {ECO:0000313|EMBL:OUS67973.1, ECO:0000313|Proteomes:UP000196208};
RN [1] {ECO:0000313|EMBL:OUS67973.1, ECO:0000313|Proteomes:UP000196208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A601 {ECO:0000313|EMBL:OUS67973.1,
RC ECO:0000313|Proteomes:UP000196208};
RA Cheng Y., Li J.G., Liu H., Han W.J.;
RT "Draft Genome of a Polysaccharide-Degrading Marine Bacterium
RT Pseudoalteromonas sp. A601.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OUS67973.1}.
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DR EMBL; MXQF01000050; OUS67973.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5JNM9; -.
DR OrthoDB; 6276619at2; -.
DR Proteomes; UP000196208; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 1.10.390.20; -; 1.
DR Gene3D; 2.60.120.380; -; 2.
DR Gene3D; 3.40.30.160; Collagenase ColT, N-terminal domain; 1.
DR InterPro; IPR007280; Peptidase_C_arc/bac.
DR InterPro; IPR002169; Peptidase_M9A/M9B.
DR Pfam; PF01752; Peptidase_M9; 1.
DR Pfam; PF04151; PPC; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..795
FT /note="Peptidase C-terminal archaeal/bacterial domain-
FT containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012034426"
FT DOMAIN 471..541
FT /note="Peptidase C-terminal archaeal/bacterial"
FT /evidence="ECO:0000259|Pfam:PF04151"
FT REGION 21..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..77
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 325
FT /evidence="ECO:0000256|PIRSR:PIRSR602169-1"
SQ SEQUENCE 795 AA; 87004 MW; 1354D14769F5F4BE CRC64;
MFFKKLTLTS AILCALSGCG GSDDSTNTLP EPTPPVTVTP ADPEVEPSDP EVEPTDPEVE
PSDPEVEPTD PEVEPTEPEV DYTSALEPAL ALDVVKTNIN TVGGEGQSFY VDLTQESETL
VVSLFAGVEN KDLGDPDLYV KYEGEASAGA EGVFDCVSYK GSNNNETCII DKPKAGRYHI
YMDAYEGGDA VDASMFATTG LFSANMMCEE PVRIRAQSMS NAELEEACTV ITQTKRLFDE
TLHSGLTPEF QQAVPDDLNE ITNIHIFSSL SNHAAWAEHL VNTNNTSGIY FETSPTQWWH
SSDIWTFDAL EWTEGRSVIR SLAHEYVHAL DGRYNKEGAY KSSVNWWTEG LAEYLGTFNE
LYYTRVSTAH DGEAASLADI FAGNADAYSW GQLAVSFLIE NHPELVYQML VHMRAGEWED
FELLLDNIAT DNQAEFTTWL STTLVDQYKE SVEVLTLGDY KQINGRGGWL FSVDVPAGLP
SITFATQGGS ASVDLWVKKG AALHPAVDTE FTCTSITEST NTENCTISMP ESGKYYIAVA
SDFVGADVVD LYFSACAGDD CAVTTPEQQA LVTVTEPYLP HWPEKGTLGT CSLAETYYNS
SKPALDLSIT NPTEKLVKVY WLNRNTGDKG GNPYVTLGQD ESYVSDDWNI GHRIMLTDGA
DNCLGVALLN DENNTFNVTE EMVVDALDEA PPAEIPEATA VMQSCDLAVP YERTSNSAPN
LQVINTMSDP VKLYWINNTT GEPALDYVYA TLAEGEIYTQ TYWAAGDRMM VTDESNSCIG
VLDLNDTDNV FVLGN
//
