ID A0A1H6MQC4_9FLAO Unreviewed; 664 AA.
AC A0A1H6MQC4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Por secretion system C-terminal sorting domain-containing protein {ECO:0000313|EMBL:SEI04080.1};
GN ORFNames=SAMN02927937_02913 {ECO:0000313|EMBL:SEI04080.1};
OS Paenimyroides aquimaris.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Paenimyroides.
OX NCBI_TaxID=1159016 {ECO:0000313|EMBL:SEI04080.1, ECO:0000313|Proteomes:UP000199634};
RN [1] {ECO:0000313|EMBL:SEI04080.1, ECO:0000313|Proteomes:UP000199634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10825 {ECO:0000313|EMBL:SEI04080.1,
RC ECO:0000313|Proteomes:UP000199634};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FNXE01000084; SEI04080.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6MQC4; -.
DR STRING; 1159016.SAMN02927937_02913; -.
DR OrthoDB; 291295at2; -.
DR Proteomes; UP000199634; Unassembled WGS sequence.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09597; M4_TLP; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 3.10.450.490; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR InterPro; IPR026444; Secre_tail.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
DR PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR Pfam; PF18962; Por_Secre_tail; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000199634};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..664
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011508173"
FT DOMAIN 85..133
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 230..385
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 392..574
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT DOMAIN 592..663
FT /note="Secretion system C-terminal sorting"
FT /evidence="ECO:0000259|Pfam:PF18962"
SQ SEQUENCE 664 AA; 73580 MW; 099205A835FC6D99 CRC64;
MNKKIFQLKK IPVVFLLSGV LLVSTNNVFA INTPIQISSY SSELPKPQYQ NGYGTFLVDA
TNTKISVSEF SNQLNDYFDL DDQHTFELVN EQRDASTGYN YYSYQHFYND VKVNGDMVFV
HAKNDQVQYI NGQIVKIAEL SVTHSIDEEK IKEVALNNFG ITENVQISKI ENFIYKQESQ
EGKISLKQVA KISLIATAPF KTIEYLIDVQ SNEIISQFDK FHKADTQSTS ATYFRGNQSI
TVDSYNGSYR LKDNARNIRT LNAVNLTGHL NADGTFSGYS EYTNSSANFT SVNTKPAVEV
HWAMKNTYDY YKNIHNRTSF DGNGHAINNY YDAGTALGTH ENAAALDEVD NGYELIGMFY
GKGGSYLHPV VGLDVAGHEF SHMVVSRNGN GGLDYQNESG ALNESFADMF GTSIEFYVND
NPNWTIGEGL LKSSSITPNY FRSMSNPNSA PTSIGMPSQP DTYKGQYWQN TTNNPNGYND
YGGVHINSGV GNHWFYLLSE GGSGVNDINK SYNVTGITIQ KAEKIAYRAL TTGLSSSATY
LDAYNATIAA AAALYGANSN EWTQVVDAWY AVGIGSGAAS TKNYEMEAKL KVYPNPVTGD
EVTIESNLDE TTTVEMFDLT GKQVLAPKQI ESRTVLNTSN YKTGVYILKF KSTLGEYSHK
LIIK
//