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Database: UniProt
Entry: D0S1F8_ACICA
LinkDB: D0S1F8_ACICA
Original site: D0S1F8_ACICA 
ID   D0S1F8_ACICA            Unreviewed;       476 AA.
AC   D0S1F8;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   SubName: Full=Serine protease MucD {ECO:0000313|EMBL:EEY77275.1};
DE            EC=3.4.21.- {ECO:0000313|EMBL:EEY77275.1};
GN   Name=mucD {ECO:0000313|EMBL:EEY77275.1};
GN   ORFNames=HMPREF0012_00144 {ECO:0000313|EMBL:EEY77275.1};
OS   Acinetobacter calcoaceticus RUH2202.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=575585 {ECO:0000313|EMBL:EEY77275.1, ECO:0000313|Proteomes:UP000005126};
RN   [1] {ECO:0000313|Proteomes:UP000005126}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RUH2202 {ECO:0000313|Proteomes:UP000005126};
RX   PubMed=23144699; DOI=10.1371/journal.pone.0046984;
RA   Peleg A.Y., de Breij A., Adams M.D., Cerqueira G.M., Mocali S.,
RA   Galardini M., Nibbering P.H., Earl A.M., Ward D.V., Paterson D.L.,
RA   Seifert H., Dijkshoorn L.;
RT   "The success of Acinetobacter species; genetic, metabolic and virulence
RT   attributes.";
RL   PLoS ONE 7:E46984-E46984(2012).
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DR   EMBL; GG704949; EEY77275.1; -; Genomic_DNA.
DR   AlphaFoldDB; D0S1F8; -.
DR   HOGENOM; CLU_020120_1_0_6; -.
DR   Proteomes; UP000005126; Unassembled WGS sequence.
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; 2.
DR   Gene3D; 2.30.42.10; -; 2.
DR   Gene3D; 2.40.10.120; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR011782; Pept_S1C_Do.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001940; Peptidase_S1C.
DR   NCBIfam; TIGR02037; degP_htrA_DO; 1.
DR   PANTHER; PTHR22939; SERINE PROTEASE FAMILY S1C HTRA-RELATED; 1.
DR   PANTHER; PTHR22939:SF129; SERINE PROTEASE HTRA2, MITOCHONDRIAL; 1.
DR   Pfam; PF13180; PDZ_2; 2.
DR   Pfam; PF13365; Trypsin_2; 1.
DR   PRINTS; PR00834; PROTEASES2C.
DR   SMART; SM00228; PDZ; 2.
DR   SUPFAM; SSF50156; PDZ domain-like; 2.
DR   SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR   PROSITE; PS50106; PDZ; 2.
PE   4: Predicted;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EEY77275.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:EEY77275.1};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          261..331
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          383..454
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   ACT_SITE        119
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT   ACT_SITE        149
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
FT   ACT_SITE        222
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR611782-1"
SQ   SEQUENCE   476 AA;  51488 MW;  3CC5FC318992F81E CRC64;
     MIQQFYSYSR RPIVGEHQMK TRYLQQGMYA AVFTVAAVQA NATVDFSNLV EQVSPAVVSV
     NVVKKMTQDE LLQQQVPEIL KRFFGNQVII PQQQGPQEKT AYGSAFFISK DGYLLTNHHV
     IENASRISIT LNDRREIDAT VVGSDERTDV ALLKVTGNSY PALKVGNVDR LRVGEPVLAI
     GSPFGFDYSA SAGIVSAKSR NMSGETSIPF IQTDVALNPG NSGGPLFNQN GEVVGVNSRI
     FSGTGGYMGL SFSIPIDVAM DVAEQLKTKG KVTRSYLGVM MQDIDRNLAD AYKLPKPEGA
     LITQISPNSP AQKAGLRAGD VILKYNGNPV SRTSELLYAL NKVQPNQTIQ FEVLRDDKTR
     NISATLTTAP DETPATGAQS AVSKGPVLGM SIRDLAEPEK SALSVKGGIY VQDVRRGGLA
     SLSNIIPGDV IVQVNNNQIL NSQDFAKVVS NLQKNTVARV AIIRQGQRAM LGLRIQ
//
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