ID L0WAZ7_9GAMM Unreviewed; 381 AA.
AC L0WAZ7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Serine endopeptidase {ECO:0000313|EMBL:EKF74189.1};
GN ORFNames=A11A3_10232 {ECO:0000313|EMBL:EKF74189.1};
OS Alcanivorax hongdengensis A-11-3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=1177179 {ECO:0000313|EMBL:EKF74189.1, ECO:0000313|Proteomes:UP000010164};
RN [1] {ECO:0000313|EMBL:EKF74189.1, ECO:0000313|Proteomes:UP000010164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A-11-3 {ECO:0000313|EMBL:EKF74189.1,
RC ECO:0000313|Proteomes:UP000010164};
RX PubMed=23209226; DOI=10.1128/JB.01849-12;
RA Lai Q., Shao Z.;
RT "Genome Sequence of the Alkane-Degrading Bacterium Alcanivorax
RT hongdengensis Type Strain A-11-3.";
RL J. Bacteriol. 194:6972-6972(2012).
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:EKF74189.1}.
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DR EMBL; AMRJ01000014; EKF74189.1; -; Genomic_DNA.
DR RefSeq; WP_008929224.1; NZ_AMRJ01000014.1.
DR AlphaFoldDB; L0WAZ7; -.
DR STRING; 1177179.A11A3_10232; -.
DR MEROPS; S01.477; -.
DR PATRIC; fig|1177179.3.peg.2038; -.
DR eggNOG; COG0265; Bacteria.
DR Proteomes; UP000010164; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00987; PDZ_serine_protease; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.120; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR22939:SF101; PERIPLASMIC PH-DEPENDENT SERINE ENDOPROTEASE DEGQ; 1.
DR PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 256..320
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 354..381
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..381
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 381 AA; 40319 MW; E88B0CA7BA99EAF0 CRC64;
MKLIRFLAAP VLTGLAVGLV ALWWYQWGPQ SSHSRPSPAV DSYADAVNLA APAVVNIYTT
QIVTTEKDVS KDPLFNRFME RPRRERALSS LGSGVIVADN GYVLTSYHVI RDADEILVAL
RDGRDAPARV VGTDPETDLA LLQIALEKLP KIELNGDGPV QVGDVVLAIG NPLGVGQTVS
MGIVSATGRS HLGIATFENF IQTDAAINRG NSGGALIDTR GHLIGINTAI LSADGNWQGI
GFATPASIAK EVMDDLIKHG RVIRGYLGVT VQDMTPSLAE TFGLDNVHGG VVTEVVVDSP
ANRAGLQPGD VLVGIDGQAM ADGYEAMNRI AGMKPGTETT LNLIRNRKAV DADVTIGTRP
PAKTRDDDRE EDASAQQDGG E
//