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Database: UniProt
Entry: A0A083ZW44_9GAMM
LinkDB: A0A083ZW44_9GAMM
Original site: A0A083ZW44_9GAMM 
ID   A0A083ZW44_9GAMM        Unreviewed;      1006 AA.
AC   A0A083ZW44;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   02-APR-2025, entry version 30.
DE   SubName: Full=Extracellular serine protease {ECO:0000313|EMBL:KEY57273.1};
DE            EC=3.4.21.- {ECO:0000313|EMBL:KEY57273.1};
GN   ORFNames=SRDD_37660 {ECO:0000313|EMBL:KEY57273.1};
OS   Serratia sp. DD3.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Yersiniaceae; Serratia.
OX   NCBI_TaxID=1410619 {ECO:0000313|EMBL:KEY57273.1, ECO:0000313|Proteomes:UP000017810};
RN   [1] {ECO:0000313|EMBL:KEY57273.1, ECO:0000313|Proteomes:UP000017810}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DD3 {ECO:0000313|EMBL:KEY57273.1,
RC   ECO:0000313|Proteomes:UP000017810};
RX   PubMed=25212623;
RA   Poehlein A., Freese H.M., Daniel R., Simeonova D.D.;
RT   "Draft Genome Sequence of Serratia sp. Strain DD3, Isolated from the Guts
RT   of Daphnia magna.";
RL   Genome Announc. 2:e00903-14(2014).
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:KEY57273.1}.
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DR   EMBL; AYKS02000093; KEY57273.1; -; Genomic_DNA.
DR   RefSeq; WP_023490344.1; NZ_AYKS02000093.1.
DR   AlphaFoldDB; A0A083ZW44; -.
DR   STRING; 1410619.SRDD_37660; -.
DR   eggNOG; COG0671; Bacteria.
DR   eggNOG; COG4625; Bacteria.
DR   Proteomes; UP000017810; Unassembled WGS sequence.
DR   GO; GO:0019867; C:outer membrane; IEA:InterPro.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IEA:InterPro.
DR   GO; GO:0003993; F:acid phosphatase activity; IEA:InterPro.
DR   GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.128.130; Autotransporter beta-domain; 1.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR   InterPro; IPR001011; Acid_Pase_classA_bac.
DR   InterPro; IPR005546; Autotransporte_beta.
DR   InterPro; IPR036709; Autotransporte_beta_dom_sf.
DR   InterPro; IPR013425; Autotrns_rpt.
DR   InterPro; IPR006315; OM_autotransptr_brl_dom.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR   InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR   NCBIfam; TIGR01414; autotrans_barl; 1.
DR   NCBIfam; TIGR02601; autotrns_rpt; 1.
DR   Pfam; PF03797; Autotransporter; 1.
DR   Pfam; PF01569; PAP2; 1.
DR   Pfam; PF12951; PATR; 1.
DR   PRINTS; PR00483; BACPHPHTASE.
DR   SMART; SM00014; acidPPc; 1.
DR   SMART; SM00869; Autotransporter; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
DR   SUPFAM; SSF103515; Autotransporter; 1.
DR   SUPFAM; SSF51126; Pectin lyase-like; 1.
DR   PROSITE; PS51208; AUTOTRANSPORTER; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:KEY57273.1};
KW   Protease {ECO:0000313|EMBL:KEY57273.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017810};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..1006
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001770329"
FT   DOMAIN          734..1006
FT                   /note="Autotransporter"
FT                   /evidence="ECO:0000259|PROSITE:PS51208"
SQ   SEQUENCE   1006 AA;  106189 MW;  869C62A6876EF3A1 CRC64;
     MSKKTALSAL SIAILLSLNT AWAIEARTIQ ATELISGFSL LNNSTAGQTV LNDNLNTSIA
     TNNNASDAVR ARAIADNTIA ALIGSISNGL LVANALGPKM YGTFASANSI NATNYTATTF
     SKNFEALFSQ VNALIQVDSS FAKNYYANGS ANGKPAQLAT GISLPAGGVY NVYDLAYHPS
     DANRNTIGNS RPVQVAPDSI DTFSAPDFFG VETDSAVAII PTLKSNAAFP SGHAAFGFAS
     TLLFAEMVPE RFQEFLLRGS EYGNSRMVLG AHYALDVIGA RIMTTYALAQ ILNNNPDYLG
     QNIASILGAP MVTSTDFQGL MQAAQTDLRS LLEQGCQSTF AECSAADQAQ RQAVAAQNKA
     DYRYRMTYGL AVIGPTDLAP VVPEGAEVLI ASRFPYLTAE QRRDVLATTE IESGHALDDG
     SGWARINLYD AADGYGAFNG NITVNMDANQ GGFSAYDVWA NDIAGNGNFV KNGSGVLEFT
     GNNSFSGSTT VAGGALIING YYGNSAVTVD NGALLGGSGT VGALTAQSGA IIAPGNSIGT
     LQVANNVTFQ PGARYAVEIA TDGRSDQIQS QGMAILNGAD VLVSLEHSGN LLSQNEVHSL
     LGHQYTILSA QLGVQGQFDT VQPDYLFLGT TLNYQPTQVT LNVGRNTTAF ADMALTPNQR
     ALATAADTLP AGNPVYESIL TSQSAWEAQQ AYRRLSGQIH ADMASAQIND SRYLRDALNE
     RLRQSEGLTH SPDIKVNEGG AWAQFLGAWD HASGDTNATG YQASTYGILM GLDSTLAQQW
     QLGVTSGYTR TSLDGGYGSN ATSDNYHLGV YGGKQLDNLA LRAGSTYTWH RIETSRNVNY
     ATQFDNPSAN YSARTQQLFA EAGYSIQAST VKLEPFANLA YINYQNNGIA ENGGAAALHG
     DKQHTDATAS TLGMRADTQL QAVTLRGELG WQHQYGDSDR GIGLMFSGSS VPFVNNSVPV
     SRDAAVVKAN AEVAVGNNAT LSLGYGGLVS SSHQDNRVNA GFTWHF
//
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