ID   A0A1H9F6Z0_9LACT        Unreviewed;      1130 AA.
AC   A0A1H9F6Z0;
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=LPXTG-motif cell wall anchor domain-containing protein {ECO:0000313|EMBL:SEQ33736.1};
GN   ORFNames=SAMN04488558_10894 {ECO:0000313|EMBL:SEQ33736.1};
OS   Ignavigranum ruoffiae.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Ignavigranum.
OX   NCBI_TaxID=89093 {ECO:0000313|EMBL:SEQ33736.1, ECO:0000313|Proteomes:UP000198833};
RN   [1] {ECO:0000313|EMBL:SEQ33736.1, ECO:0000313|Proteomes:UP000198833}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15695 {ECO:0000313|EMBL:SEQ33736.1,
RC   ECO:0000313|Proteomes:UP000198833};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the serine-aspartate repeat-containing protein
CC       (SDr) family. {ECO:0000256|ARBA:ARBA00007257}.
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DR   EMBL; FOEN01000008; SEQ33736.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9F6Z0; -.
DR   STRING; 89093.SAMN04488558_10894; -.
DR   OrthoDB; 2139979at2; -.
DR   Proteomes; UP000198833; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   Gene3D; 2.60.40.1120; Carboxypeptidase-like, regulatory domain; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 5.
DR   InterPro; IPR013784; Carb-bd-like_fold.
DR   InterPro; IPR008969; CarboxyPept-like_regulatory.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR019931; LPXTG_anchor.
DR   NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR   PANTHER; PTHR36108:SF13; COLOSSIN-B; 1.
DR   PANTHER; PTHR36108; COLOSSIN-B-RELATED; 1.
DR   Pfam; PF13620; CarboxypepD_reg; 1.
DR   Pfam; PF00746; Gram_pos_anchor; 1.
DR   SUPFAM; SSF49464; Carboxypeptidase regulatory domain-like; 1.
DR   SUPFAM; SSF49452; Starch-binding domain-like; 1.
PE   3: Inferred from homology;
KW   Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198833};
KW   Secreted {ECO:0000256|ARBA:ARBA00022512};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        1100..1118
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1086..1124
FT                   /note="Gram-positive cocci surface proteins LPxTG"
FT                   /evidence="ECO:0000259|Pfam:PF00746"
FT   REGION          178..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          879..936
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1060..1093
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        879..922
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1060..1075
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1076..1090
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1130 AA;  123161 MW;  8CA892D077533DEE CRC64;
     MKKITRWINS IILFLSVMFP LVQVSAQEEM VKFNLDLSLI VEGSEPITQN EYRFDIIERN
     ADQSAFEGAA VYKYDSTDPN QQAEIYLPAG VYTFRLYDGA SEPFHREGQA LSLDTALQTD
     EADASGQQMK PTLNQGSLND WGNGTLVYDI NFVVQPGPGL INSDTGEQEI TLQLIFSTEG
     EDASSEETSS EESENTTIDP SDPNAPAVSE IEVPFKVVDQ DGQAVEGVQI TVNGQTLTTD
     ENGEAQTGLA PGNMDIVISN LPEGYTGGGA YNPIALTEDL NGPIEFTIQK TEVTAPVIFT
     AVDEQGQGIA GVGIQLLDHE VMTDGQGQVR IDQVPVGQQT YTVSSQPQGY SIEPTTAEFE
     VLADQENTVN LNFQTEVQTG MASIQVYDQY QDPVVGLGIT IAGQEYLSDN NGLIEIKDLA
     AQEHAYQVTT VPTGYQQPDD GIITVEAGVE TDTTLNVIKD AQPGIVQLKI IDQDDQGVAQ
     AEVLVEDQSY SSDDQGLIEI KDLSPGTYNY QLLSLPQGYQ GQKSGVITVT EDQTTEEVLK
     VERDLATGQF TLIVKDQDGQ AVEGAIVSLA DKSTPTDSQG QAIFSQLTPD TYDYEIQVLP
     EGYEQNIGSQ SIAIREGAQE ERTVTVEKVP AKGQLTITAL DQADQPVAGV VVKVADKLIR
     TDQEGQAVLK DLAPDTYTYQ INQFPPKYSG KDTGQVTIPA GEDASLHIYL EKEIKPAKAT
     LTVLDQNQEP VAGVSIQFGG LQAETNADGQ IVFEELSPGV YNYTMIDVPK GYSFEASNEQ
     AELKEEDDFQ DKFQIEKLPE QGKVKVRLTD QDGKGIAGAR VKLSGKESTT DKDGYVEFSA
     VNVGEASVEV LELPQGYQLD QKTQTITVKQ DQTVDLSFTA QAPESQTSES EQETTTSSAE
     STTSQTSQES TEITTTTETQ TIKETEVDPE QEASIESEAA QATRQFVDAN SGIEVWVNPQ
     DAKQVVKLTV DKLKTSDFAS LKDYDADVYQ LTLLDKNNQA VDLTKIAEVK IPTRPVNSQI
     KVLRLDQDQL SSLTFALQNR RVTYRTQKLG NFAVTYGNKA QASGTEESTT TEKSQNVQVD
     KEKSVEKKGD LPGTGEQTQT MIVILALALL LGAAYLFVRH NRSQKDDRQE
//