ID A0A1Y5RS14_9RHOB Unreviewed; 1617 AA.
AC A0A1Y5RS14;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Microbial collagenase {ECO:0000313|EMBL:SLN24013.1};
DE EC=3.4.24.3 {ECO:0000313|EMBL:SLN24013.1};
GN Name=colA {ECO:0000313|EMBL:SLN24013.1};
GN ORFNames=TRL7639_00768 {ECO:0000313|EMBL:SLN24013.1};
OS Falsiruegeria litorea R37.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Falsiruegeria.
OX NCBI_TaxID=1200284 {ECO:0000313|EMBL:SLN24013.1, ECO:0000313|Proteomes:UP000193077};
RN [1] {ECO:0000313|EMBL:SLN24013.1, ECO:0000313|Proteomes:UP000193077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7639 {ECO:0000313|EMBL:SLN24013.1,
RC ECO:0000313|Proteomes:UP000193077};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FWFO01000001; SLN24013.1; -; Genomic_DNA.
DR OrthoDB; 9773411at2; -.
DR Proteomes; UP000193077; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR CDD; cd00146; PKD; 12.
DR Gene3D; 2.60.40.10; Immunoglobulins; 15.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR022409; PKD/Chitinase_dom.
DR InterPro; IPR000601; PKD_dom.
DR InterPro; IPR035986; PKD_dom_sf.
DR PANTHER; PTHR46730:SF1; PLAT DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46730; POLYCYSTIN-1; 1.
DR Pfam; PF18911; PKD_4; 15.
DR SMART; SM00089; PKD; 15.
DR SUPFAM; SSF49299; PKD domain; 14.
DR PROSITE; PS50093; PKD; 15.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:SLN24013.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000193077};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}; Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1617
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012124908"
FT DOMAIN 339..376
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 423..465
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 483..553
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 600..650
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 673..731
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 744..831
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 831..909
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 947..989
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1006..1076
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1093..1162
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1215..1253
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1269..1339
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1387..1421
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1438..1508
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT DOMAIN 1540..1599
FT /note="PKD"
FT /evidence="ECO:0000259|PROSITE:PS50093"
FT REGION 103..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1617 AA; 170737 MW; AF947209243EAA7F CRC64;
MWWMKGCAAA ALAMVLSSVQ LVAQPAPVSD GLLVVYGPLA PAREGDVDRR EQVFFSIPAD
LKDRVYVRIF DPEIAGDNDF TYGGPGDSET TFRVFGGDGA FTDADRPEPV EDGAREPRLI
PYDPVTQPGK LIKEKAWTSD RDTDGRWVNL TALRARQGEV VEGRAYFRID VQGSKGNDGN
GYTLGVSLSR DRARPPEGLE MFAYRPTVRW SAGSTATQVW FTRTTDGPFQ VQSFDGANGE
LALVTDYGDL GLRISGQNFW TSDSVDTEET NLAISLLGGF ETPNDVTLAV FDAAGDPVPL
DMPPKHAPEP ARPTAIGTGR PLADCRSVAF DGNGSIGLTP LGFDWDFGDG NRSSEPVVAH
RYAAPGRYTA RLRVLDPGTR PGRGDEVSVP VHIRNAPVAV PGSDIVVAPG QVVAFDGSNS
QPSDGPITSY GWSFGDGGRA QGAKTSYVYK TPGQYRAVLR VKDDAEHPCN VGLATRRVTV
NFAPVAEAGT DQSAIIGQTI IVSAGASYDV DGLINTYRWS MGDGTVLEGE TVTHQYAESG
SYQVLLTVID DSGVANNLAT DGMRITVNAP PEPSFIIPDR PVSVSELAML DGTASLDTDG
QILSYIWDFG DGAMGEGPIV DYAWTRAGEY TVTLTVEDDS GTASALQSVT RIVRVDAAPV
ADAGADQFVT ASEVTFSGGG SVDPDGAVTE WLWEFGDGGT ASGQNVKHAY LRPGTYEVAL
TVRDDSGAPL NTDRDTMRVT INATPIADAG PPQVVAPGEE FVVSGRASVD PDGEVSEYLW
TFPDGQTVSG LRAAHTINEP GLYRIGLVVR DNFQGGAAED EAEVFITVNA PPVAVAGADR
LIAPGDSLQF DAGQSFDSDG RVTSYRWEFD DLGDPLEART VERHYPTAGV WSAQLVVTDD
SGVLNSTASD DMTIRVNHPP VAEAGPDIDT DKLYVAFDAS QSKDADGDAL MYVWDFGDGS
TAAYGEQVTH VYPRSGVFPV TLRVDDGTGL SNARAIDATR VTIRARPMAD AGGNRDVCSG
EPILFDASDS ADPDGGLLLY EWDFGDGSGS DLINPTKTFE LPGVYPVTLT VRNETGTQYG
TDIDRIAALV REGPIADAGG DRTVCSNQQV RFDGSGSTDA DGAVNAFSWT FGDGNTGSGE
NPVHIFKRPG TYAVTLTITG EARGACSPLD SDVANIIVVA APTLEIAGPD RAAAGLPATF
RAELGQLGGA QAQGFSWEVS DGTTMQGGEL VHTFAEPGEY LVTLRSNLTG GTAGCTDLEV
VRKVIVNAPP EPVIDVVAEV AVGQAVRFDG GGSSDPDGAI TRFRWEFGDG NAADTVLTSH
RFAEPGDKTV VLTVWDDAGV GNSEQRVEKI VRVTPAPVAG LVADGAVCPG VDTPWSVGVA
EGTQVIWTFG DGTQATGASV DHVFAAPGQY PVRVRMDDGR GLLSSQRNEE AYVRVNSEPT
ALAGPDRIVC PGDVVRFDAS ASGDLDGQIT DWSWEFSDGV ILEGERVERV FDSPADLMVR
LRVRDDSGAL GCDVGTDAAR VLVNAPPIVD AGPDRTVPVG AAHDVVRFAE ENARDPDGQG
TQVTWAFGDG TEARGAVVRH RYATPGSYTV TVRAQDSTGL TCGIGRDTAT ITAIARE
//
